Lipids- definition, properties, structure, types, examples,

functions

Lipids definition
• Lipids are a heterogeneous group of organic compounds that are insoluble in
water and soluble in non-polar organic solvents.
• They naturally occur in most plants, animals, microorganisms and are used as
cell membrane components, energy storage molecules, insulation, and
hormones.

Properties of Lipids
• Lipids may be either liquids or non-crystalline solids at room temperature.
• Pure fats and oils are colorless, odorless, and tasteless.
• They are energy-rich organic molecules
• Insoluble in water
• Soluble in organic solvents like alcohol, chloroform, acetone, benzene, etc.
• No ionic charges
• Solid triglycerols (Fats) have high proportions of saturated fatty acids.
• Liquid triglycerols (Oils) have high proportions of unsaturated fatty acids.
1. Hydrolysis of triglycerols
Triglycerols like any other esters react with water to form their carboxylic acid and
alcohol– a process known as hydrolysis.
2. Saponification:
Triacylglycerols may be hydrolyzed by several procedures, the most common of
which utilizes alkali or enzymes called lipases. Alkaline hydrolysis is termed
saponification because one of the products of the hydrolysis is a soap, generally
sodium or potassium salts of fatty acids.
3. Hydrogenation
The carbon-carbon double bonds in unsaturated fatty acids can be hydrogenated
by reacting with hydrogen to produce saturated fatty acids.
4. Halogenation
Unsaturated fatty acids, whether they are free or combined as esters in fats and
oils, react with halogens by addition at the double bond(s). The reaction results in
the decolorization of the halogen solution.
5. Rancidity:
The term rancid is applied to any fat or oil that develops a disagreeable odor.
Hydrolysis and oxidation reactions are responsible for causing rancidity. Oxidative
rancidity occurs in triacylglycerols containing unsaturated fatty acids.

Structure of Lipids
• Lipids are made of the elements Carbon, Hydrogen and Oxygen, but have a
much lower proportion of water than other molecules such as carbohydrates.
• Unlike polysaccharides and proteins, lipids are not polymers—they lack a
repeating monomeric unit.
• They are made from two molecules: Glycerol and Fatty Acids.
• A glycerol molecule is made up of three carbon atoms with a hydroxyl group
attached to it and hydrogen atoms occupying the remaining positions.
• Fatty acids consist of an acid group at one end of the molecule and a
hydrocarbon chain, which is usually denoted by the letter ‘R’.
• They may be saturated or unsaturated.
• A fatty acid is saturated if every possible bond is made with a Hydrogen atom,
such that there exist no C=C bonds.
• Unsaturated fatty acids, on the other hand, do contain C=C bonds.
Monounsaturated fatty acids have one C=C bond, and polyunsaturated have
more than one C=C bond.
Structure of Triglycerides
• Triglycerides are lipids consisting of one glycerol molecule bonded with three
fatty acid molecules.
• The bonds between the molecules are covalent and are called Ester bonds.
• They are formed during a condensation reaction.
• The charges are evenly distributed around the molecule so hydrogen bonds
to not form with water molecules making them insoluble in water.

Classification (Types) of Lipids

Lipids can be classified according to their hydrolysis products and according to
similarities in their molecular structures. Three major subclasses are recognized:
1. Simple lipids
(a) Fats and oils which yield fatty acids and glycerol upon hydrolysis.
(b) Waxes, which yield fatty acids and long-chain alcohols upon hydrolysis.
Fats and Oils
• Both types of compounds are called triacylglycerols because they are esters
composed of three fatty acids joined to glycerol, trihydroxy alcohol.
• The difference is on the basis of their physical states at room temperature. It
is customary to call a lipid a fat if it is solid at 25°C, and oil if it is a liquid at
the same temperature.
• These differences in melting points reflect differences in the degree of
unsaturation of the constituent fatty acids.
Waxes
• Wax is an ester of long-chain alcohol (usually mono-hydroxy) and a fatty acid.
• The acids and alcohols normally found in waxes have chains of the order of
12-34 carbon atoms in length.
2. Compound lipids
(a) Phospholipids, which yield fatty acids, glycerol, amino alcohol sphingosine,
phosphoric acid and nitrogen-containing alcohol upon hydrolysis.
They may be glycerophospholipids or sphingophospholipid depending upon the
alcohol group present (glycerol or sphingosine).
(b) Glycolipids, which yield fatty acids, sphingosine or glycerol, and a carbo-
hydrate upon hydrolysis.
They may also be glyceroglycolipids or sphingoglycolipid depending upon the
alcohol group present (glycerol or sphingosine).
3. Derived lipids:
Hydrolysis product of simple and compound lipids is called derived lipids. They
include fatty acid, glycerol, sphingosine and steroid derivatives.
Steroid derivatives are phenanthrene structures that are quite different from
lipids made up of fatty acids.

Functions
It is established that lipids play extremely important roles in the normal functions
of a cell. Not only do lipids serve as highly reduced storage forms of energy, but
they also play an intimate role in the structure of cell membrane and organellar
membranes. Lipids perform many functions, such as:
1. Energy Storage
2. Making Biological Membranes
3. Insulation
4. Protection – e.g. protecting plant leaves from drying up
5. Buoyancy
6. Acting as hormones
7. Act as the structural component of the body and provide the hydrophobic
barrier that permits partitioning of the aqueous contents of the cell and
subcellular structures.
8. Lipids are major sources of energy in animals and high lipid-containing seeds.
9. Activators of enzymes eg. glucose-6-phosphatase, stearyl CoA desaturase and
ω-monooxygenase, and β-hydroxybutyric dehydrogenase (a mitochondrial
enzyme) require phosphatidylcholine micelles for activation.
Amino Acids- Properties, Structure, Classification and
Functions

• Amino acids constitute a group of neutral products clearly distinguished from

other natural compounds chemically, mainly because of their ampholytic
properties, and biochemically, mainly because of their role as protein
constituents.
• An amino acid is a carboxylic acid-containing an aliphatic primary amino
group in the α position to the carboxyl group and with a characteristic
stereochemistry.
• Proteins are biosynthesized from 20 amino acids in a system involving strict
genetic control. Thus, amino acids are the basic unit of proteins.
• More than 300 amino acids are found in nature but only 20 amino acids are
standard and present in protein because they are coded by genes. Other
amino acids are modified amino acids and called non-protein amino acids.
• Some are residues modified after a protein has been synthesized by
posttranslational modifications; others are amino acids present in living
organisms but not as constituents of proteins.
Properties of Amino acids
Physical Properties
1. Amino acids are colorless, crystalline solid.
2. All amino acids have a high melting point greater than 200o
3. Solubility: They are soluble in water, slightly soluble in alcohol and dissolve
with difficulty in methanol, ethanol, and propanol. R-group of amino acids
and pH of the solvent play important role in solubility.
4. On heating to high temperatures, they decompose.
5. All amino acids (except glycine) are optically active.
6. Peptide bond formation: Amino acids can connect with a peptide bond
involving their amino and carboxylate groups. A covalent bond formed
between the alpha-amino group of one amino acid and an alpha-carboxyl
group of other forming -CO-NH-linkage. Peptide bonds are planar and
partially ionic.
Chemical Properties
1. Zwitterionic property
A zwitterion is a molecule with functional groups, of which at least one has a
positive and one has a negative electrical charge. The net charge of the entire
molecule is zero. Amino acids are the best-known examples of zwitterions. They
contain an amine group (basic) and a carboxylic group (acidic). The -NH2 group
is the stronger base, and so it picks up H+ from the -COOH group to leave a
zwitterion. The (neutral) zwitterion is the usual form amino acids exist in solution.
2. Amphoteric property
Amino acids are amphoteric in nature that is they act as both acids and base
since due to the two amine and carboxylic group present.
3. Ninhydrin test
When 1 ml of Ninhydrin solution is added to a 1 ml protein solution and heated,
the formation of a violet color indicates the presence of α-amino acids.
4. Xanthoproteic test
The xanthoproteic test is performed for the detection of aromatic amino acids
(tyrosine, tryptophan, and phenylalanine) in a protein solution. The nitration of
benzoid radicals present in the amino acid chain occurs due to reaction with nitric
acid, giving the solution yellow coloration.
5. Reaction with Sanger’s reagent
Sanger’s reagent (1-fluoro-2, 4-dinitrobenzene) reacts with a free amino group in
the peptide chain in a mild alkaline medium under cold conditions.
6. Reaction with nitrous acid
Nitrous acid reacts with the amino group to liberate nitrogen and form the
corresponding hydroxyl.

Structure of Amino acids

• All 20 of the common amino acids are alpha-amino acids. They contain a
carboxyl group, an amino group, and a side chain (R group), all attached to
the α-carbon.

Exceptions are:
• Glycine, which does not have a side chain. Its α-carbon contains two
hydrogens.
• Proline, in which the nitrogen is part of a ring.
• Thus, each amino acid has an amine group at one end and an acid group at
the other and a distinctive side chain. The backbone is the same for all amino
acids while the side chain differs from one amino acid to the next.
• All of the 20 amino acids except glycine are of the L-configuration, as for all
but one amino acid the α-carbon is an asymmetric carbon. Because glycine
does not contain an asymmetric carbon atom, it is not optically active and,
thus, it is neither D nor L.

Classification of amino acids on the basis of R-group

1. Nonpolar, Aliphatic amino acids: The R groups in this class of amino acids are
nonpolar and hydrophobic. Glycine, Alanine, Valine, leucine, Isoleucine,
Methionine, Proline.
2. Aromatic amino acids: Phenylalanine, tyrosine, and tryptophan, with their
aromatic side chains, are relatively nonpolar (hydrophobic). All can participate
in hydrophobic interactions.
3. Polar, Uncharged amino acids: The R groups of these amino acids are more
soluble in water, or more hydrophilic, than those of the nonpolar amino acids,
because they contain functional groups that form hydrogen bonds with
water. This class of amino acids includes serine, threonine, cysteine,
asparagine, and glutamine.
4. Acidic amino acids: Amino acids in which R-group is acidic or negatively
charged. Glutamic acid and Aspartic acid
5. Basic amino acids: Amino acids in which R-group is basic or positively
charged. Lysine, Arginine, Histidine
Classification of amino acids on the basis of nutrition

1. Essential amino acids (Nine)

Nine amino acids cannot be synthesized in the body and, therefore, must be
present in the diet in order for protein synthesis to occur.
These essential amino acids are histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan, and valine.
2. Non-essential amino acids (Eleven)
These amino acids can be synthesized in the body itself and hence not necessarily
need to be acquired through diet.
Arginine, glutamine, tyrosine, cysteine, glycine, proline, serine, ornithine, alanine,
asparagine, and aspartate.
Classification of amino acids on the basis of the metabolic
fate

1. Glucogenic amino acids: These amino acids serve as precursors gluconeogenesis

for glucose formation. Glycine, alanine, serine, aspartic acid, asparagine,
glutamic acid, glutamine, proline, valine, methionine, cysteine, histidine, and
arginine.
2. Ketogenic amino acids: These amino acids breakdown to form ketone bodies.
Leucine and Lysine.
3. Both glucogenic and ketogenic amino acids: These amino acids breakdown to
form precursors for both ketone bodies and glucose. Isoleucine,
Phenylalanine, Tryptophan, and tyrosine.

Functions of Amino acids

1. In particular, 20 very important amino acids are crucial for life as they contain
peptides and proteins and are known to be the building blocks for all living
things.
2. The linear sequence of amino acid residues in a polypeptide chain determines
the three-dimensional configuration of a protein, and the structure of a
protein determines its function.
3. Amino acids are imperative for sustaining the health of the human body. They
largely promote the:
Production of hormones
• Structure of muscles
 • Human nervous system’s healthy functioning
• The health of vital organs
• Normal cellular structure
4. The amino acids are used by various tissues to synthesize proteins and to
produce nitrogen-containing compounds (e.g., purines, heme, creatine,
epinephrine), or they are oxidized to produce energy.
5. The breakdown of both dietary and tissue proteins yields nitrogen-containing
substrates and carbon skeletons.
6. The nitrogen-containing substrates are used in the biosynthesis of purines,
pyrimidines, neurotransmitters, hormones, porphyrins, and nonessential
amino acids.
7. The carbon skeletons are used as a fuel source in the citric acid cycle, used for
gluconeogenesis, or used in fatty acid synthesis.

Proteins- Properties, Structure, Classification and Functions

• Proteins are the most abundant biological macromolecules, occurring in all

cells.
• It is also the most versatile organic molecule of the living systems and occur
in great variety; thousands of different kinds, ranging in size from relatively
small peptides to large polymers.
• Proteins are the polymers of amino acids covalently linked by the peptide
bonds.
• The building blocks of proteins are the twenty naturally occurring amino
acids.
• Thus, proteins are the polymers of amino acids.

Properties of Proteins
Solubility in Water
• The relationship of proteins with water is complex.
• The secondary structure of proteins depends largely on the interaction of
peptide bonds with water through hydrogen bonds.
• Hydrogen bonds are also formed between protein (alpha and beta structures)
and water. The protein-rich static ball is more soluble than the helical
structures.
• At the tertiary structure, water causes the orientation of the chains and
hydrophilic radicals to the outside of the molecule, while the hydrophobic
chains and radicals tend to react with each other within the molecule
(hydrophobic effect).
Denaturation and Renaturation
• Proteins can be denatured by agents such as heat and urea that cause
unfolding of polypeptide chains without causing hydrolysis of peptide bonds.
• The denaturing agents destroy secondary and tertiary structures, without
affecting the primary structure.
• If a denatured protein returns to its native state after the denaturing agent is
removed, the process is called renaturation.
Some of the denaturing agents include
Physical agents: Heat, radiation, pH
Chemical agents: Urea solution which forms new hydrogen bonds in the protein,
organic solvents, detergents.

Coagulation
When proteins are denatured by heat, they form insoluble aggregates known as
coagulum. All the proteins are not heat coagulable, only a few like the albumins,
globulins are heat coagulable.

Isoelectric point
• The isoelectric point (pI) is the pH at which the number of positive charges
equals the number of negative charges, and the overall charge on the amino
acid is zero.
• At this point, when subjected to an electric field the proteins do not move
either towards anode or cathode, hence this property is used to isolate
proteins.

Molecular Weights of Proteins

• The average molecular weight of an amino acid is taken to be 110.
• The total number of amino acids in a protein multiplied by 110 gives the
approximate molecular weight of that protein.
• Different proteins have different amino acid composition and hence their
molecular weights differ.
• The molecular weights of proteins range from 5000 to 109 Daltons.
Posttranslational modifications
• It occurs after the protein has been synthesized on the ribosome.
• Phosphorylation, glycosylation, ADP ribosylation, methylation, hydroxylation,
and acetylation affect the charge and the interactions between amino acid
residues, altering the three-dimensional configuration and, thus, the function
of the protein.

Chemical Properties
1. Biuret test:
When 2 ml of test solution is added to an equal volume of 10% NaOH and one
drop of 10% CuSO4 solution, a violet colour formation indicates the presence of
peptide linkage.
2. Ninhydrin test:
When 1 ml of Ninhydrin solution is added to 1 ml protein solution and heated,
formation of a violet colour indicates the presence of α-amino acids.
Protein Structure
• The linear sequence of amino acid residues in a polypeptide chain determines
the three-dimensional configuration of a protein, and the structure of a
protein determines its function.
• All proteins contain the elements carbon, hydrogen, oxygen, nitrogen and
sulfur some of these may also contain phosphorus, iodine, and traces of
metals like ion, copper, zinc and manganese.
• A protein may contain 20 different kinds of amino acids. Each amino acid has
an amine group at one end and an acid group at the other and a distinctive
side chain.
• The backbone is the same for all amino acids while the side chain differs from
one amino acid to the next.
The structure of proteins can be divided into four levels of organization:
1. Primary Structure
• The primary structure of a protein consists of the amino acid sequence along
the polypeptide chain.
• Amino acids are joined by peptide bonds.
• Because there are no dissociable protons in peptide bonds, the charges on a
polypeptide chain are due only to the N-terminal amino group, the C-
terminal carboxyl group, and the side chains on amino acid residues.
• The primary structure determines the further levels of organization of protein
molecules.
2. Secondary Structure
• The secondary structure includes various types of local conformations in
which the atoms of the side chains are not involved.
• Secondary structures are formed by a regular repeating pattern of hydrogen
bond formation between backbone atoms.
• The secondary structure involves α-helices, β-sheets, and other types of
folding patterns that occur due to a regular repeating pattern of hydrogen
bond formation.
• The secondary structure of protein could be :
1. Alpha-helix
2. Beta-helix
• The α-helix is a right-handed coiled strand.
• The side-chain substituents of the amino acid groups in an α-helix extend to
the outside.
• Hydrogen bonds form between the oxygen of the C=O of each peptide bond
in the strand and the hydrogen of the N-H group of the peptide bond four
amino acids below it in the helix.
• The side-chain substituents of the amino acids fit in beside the N-H groups.
• The hydrogen bonding in a ß-sheet is between strands (inter-strand) rather
than within strands (intra-strand).
• The sheet conformation consists of pairs of strands lying side-by-side.
• The carbonyl oxygens in one strand hydrogen bond with the amino
hydrogens of the adjacent strand.
• The two strands can be either parallel or anti-parallel depending on whether
the strand directions (N-terminus to C-terminus) are the same or opposite.
• The anti-parallel ß-sheet is more stable due to the more well-aligned
hydrogen bonds.
3. Tertiary Structure
• Tertiary structure of a protein refers to its overall three-dimensional
conformation.
• The types of interactions between amino acid residues that produce the
three-dimensional shape of a protein include hydrophobic interactions,
electrostatic interactions, and hydrogen bonds, all of which are non-covalent.
• Covalent disulfide bonds also occur.
• It is produced by interactions between amino acid residues that may be
located at a considerable distance from each other in the primary sequence of
the polypeptide chain.
• Hydrophobic amino acid residues tend to collect in the interior of globular
proteins, where they exclude water, whereas hydrophilic residues are usually
found on the surface, where they interact with water.
4. Quaternary Structure
• Quaternary structure refers to the interaction of one or more subunits to form
a functional protein, using the same forces that stabilize the tertiary structure.
• It is the spatial arrangement of subunits in a protein that consists of more
than one polypeptide chain.

Classification of Proteins
Based on the chemical nature, structure, shape and solubility, proteins are
classified as:
1. Simple proteins: They are composed of only amino acid residue. On hydrolysis
these proteins yield only constituent amino acids. It is further divided into:
• Fibrous protein: Keratin, Elastin, Collagen
• Globular protein: Albumin, Globulin, Glutelin, Histones
2. Conjugated proteins: They are combined with non-protein moiety. Eg.
Nucleoprotein, Phosphoprotein, Lipoprotein, Metalloprotein etc.
3. Derived proteins: They are derivatives or degraded products of simple and
conjugated proteins. They may be :
• Primary derived protein: Proteans, Metaproteins, Coagulated proteins
• Secondary derived proteins: Proteosesn or albunoses, peptones, peptides.

Functions of Proteins
Proteins are vital for the growth and repair, and their functions are endless. They
also have enormous diversity of biological function and are the most important
final products of the information pathways.
• Proteins, which are composed of amino acids, serve in many roles in the body
(e.g., as enzymes, structural components, hormones, and antibodies).
• They act as structural components such as keratin of hair and nail, collagen of
bone etc.
• Proteins are the molecular instruments through which genetic information is
expressed.
• They execute their activities in the transport of oxygen and carbon dioxide by
hemoglobin and special enzymes in the red cells.
• They function in the homostatic control of the volume of the circulating blood
and that of the interstitial fluids through the plasma proteins.
• They are involved in blood clotting through thrombin, fibrinogen and other
protein factors.
• They act as the defence against infections by means of protein antibodies.
• They perform hereditary transmission by nucleoproteins of the cell nucleus.
• Ovalbumine, glutelin etc. are storage proteins.
• Actin, myosin act as contractile protein important for muscle contraction.
Biological Oxidation

This article gives the answer to the question as to “How do the food
we take in and the oxygen we respire, produce energy to
continue the process of life”. The simplest answer is that the food
we take in is oxidized by the enzymes present in the body.
During this process some reducing equivalents viz. NADH and
FADH2 are produced which are electron rich in nature. These reducing
equivalents donate their electrons to the oxygen we respire in, during
which energy is released to produce adenosine triphosphate (ATP).
ATP is known as the energy currency of the cell and it brings about the
biological process of life. In order to understand the above process, we
need to understand some basic terminologies.

Oxidation and reduction can be defined in three different

ways as under:
i. Oxidation is ‘Addition of oxygen’ or ‘removal of hydrogen’ or
‘removal of electrons’.

ii. Reduction is ‘Removal of oxygen’ or ‘addition of hydrogen’ or

‘addition of electrons’.

Oxidizing agent or oxidant:

An electron acceptor is an oxidizing agent or oxidant.

Reducing agent or reductant:

An electron donor is a reducing agent or reductant.

Redox potential (E0):

The relative tendency of reductant to donate electrons as compared to
hydrogen is termed as oxidation-reduction potential or ‘redox
potential’ (E0).
The redox potential of hydrogen is taken as zero at pH 0 (-0.417), 25°
C, in a solution of 1 molar concentration (1.0 atom of hydrogen).
i. A compound having a negative value of E0 is a better electron donor
than hydrogen.
ii. A compound having a positive value of E0 is a poor electron donor
than hydrogen.
The electrons flow from compounds with negative value of redox
potential to those with positive values of redox potential, because
there will be loss of energy and thus, the compound becomes stable.

Free energy (F0):

Every chemical substance has a certain amount of energy built into it,
which is the energy of the chemical bonds holding the atoms together.
This is the free energy.

High energy compounds and energy rich bond (~):

Any bond, which on hydrolysis gives a minimum free energy of 7.4
Kcal/mol, is known as energy rich bond and the compound which has
an energy rich bond is known as high energy compound. Ex. ATP,
pyrophosphate, 1, 3-diphosphoglyceric acid, phosphoenol pyruvate,
creatine phosphate and acetyl-CoA.

Adenosine triphosphate (ATP):

ATP is also known as the ‘energy currency’ of the living cell, because it
transfers energy from energy yielding sources to the energy requiring
cell processes. ATP has two pyrophosphate bonds. On hydrolysis of
each of the terminal two phosphate groups there is release of more
than 7.4 Kcal/mol of energy but the third bond yields only 3 Kcal/mol
of energy, hence it is not a high energy bond. On hydrolysis ATP is
converted to ADP and to AMP.

Biological oxidation:
Biological oxidation is catalysed by enzymes which function in
combination with coenzymes and/or electron carrier proteins.

Different enzymes associated with biological oxidation are:

1. Oxidoreductases:
These enzymes catalyse the removal of hydrogen from the substrate
and add it to another substance, thus bringing about oxidation
reduction reaction. Ex. Glyceraldehyde—3—
Phosphate dehydrogenase.

2. Oxidases:
These enzymes catalyse the removal of hydrogen from the substrate
and add directly to the molecular oxygen. Ex. Cytochrome oxidases,
tyrosinase, uricase.

3. Oxygenases:
These enzymes incorporate oxygen into the substrates.

(a) Mono-oxygenases:
Adds only one atom of oxygen to the substrate. These are also known
as mixed function oxidases.

(b) Di-oxygenases:
Adds both the atoms of oxygen to the substrate. Ex. Homogentisic acid
di-oxygenase.

4. Aerobic dehydrogenases:
These enzymes remove hydrogen from the substrate and add it either
directly to oxygen or any other artificial acceptors like methylene blue.
The product formed is hydrogen peroxide.

5. Anaerobic dehydrogenases:
These enzymes use other substrates or substances to donate the
hydrogen. They transfer hydrogen’s to some other hydrogen acceptor,
but not directly to oxygen. Thus the hydrogen acceptors are NAD, FAD
and FMN. Heme proteins like cytochromes also receive hydrogen’s.
The cytochromes are ‘b’, ‘c1‘, ‘c’, ‘a’ and ‘a3‘.
6. Hydro peroxidases:
These enzymes have either hydrogen peroxide (H2O2) or organic
peroxide as their substrate.
There are two types of hydro peroxidases:
(1) Peroxidase and

(2) Catalase.

Their prime function is destruction of H2O2.

Electron Transport Chain:
When electrons are transferred from the most electronegative system
[(NADH or FADH2) (-0.32V)] to the most electropositive system
(+0.82V) (Oxygen), there will be liberation of all the energy at one
time in an explosive manner. But, if they are transferred in a step wise
manner through some intermediate systems then there will be slow
release of energy and it can be captured by the cell to synthesize
energy rich compounds. During biological oxidation, electrons are
transferred through electron transport proteins which are arranged in
a specific chain to form the electron transport chain (ETC), which is
situated in the inner mitochondrial membrane.
Respiratory Chain or ETC:
Transfer of electrons from substrate to molecular oxygen through a
chain of electron carriers is called electron transport chain or
respiratory chain. Mitochondria contains a series of catalysts forming
the respiratory chain which are involved in the transfer of electrons
and hydrogen and their final reaction is with oxygen to form water.
The components of respiratory chain are arranged sequentially in the
order of increasing redox potential.

Electrons flow through the chain in a stepwise manner from lower

redox potential to higher redox potential. Some amount of energy is
liberated with transfer of electron from one component to another.
Whenever there is a release of 7.4 Kcal of energy or a little more, then
ATP formation takes place there. NADH forms 3 ATPs whereas
FADH2 forms only 2 as it enters ETC at the site beyond the first site of
ATP formation.

The/three sites of ATP formation in the ETC or respiratory

chain are:
1. Between NADH dehydrogenase (flavoprotein) and ubiquinone
(coenzyme Q).

2. Between cytochrome-b and cytochrome-c1.

3. Between cytochrome-a and cytochrome-a3 (cytochromes oxidase).
The components of ETC, their redox potential and their
sequence is:

Phosphorylation:
Esterification of a phosphate through a high energy bond (7.4 Kcal) is
known as phosphorylation. Combination of inorganic phosphate (Pi)
with any other compound through high energy bond is known as
phosphorylation. Or formation of ATP from ADP and phosphate or
NTP from NDP and Pi is known as phosphorylation.
There are two types of phosphorylation:
1. Substrate level phosphorylation:
Formation of high energy phosphate bond at the level of a substrate
without the involvement of the respiratory chain is known as substrate
level phosphorylation. Ex. Phosphoenolpyruvate is converted to
pyruvate by pyruvate kinase where ATP is formed from ADP.

2. Oxidative phosphorylation:
The enzymatic phosphorylation of ADP to ATP coupled with electron
transport from a substrate to molecular oxygen is known as oxidative
phosphorylation or respiratory chain phosphorylation.

Mechanism of Oxidative Phosphorylation:

There are three theories or hypothesis, explaining the formation of
ATP through electron transport chain.

They are as follows:

1. Chemical coupling hypothesis:
It states that a high energy compound is formed taking the energy
liberated by electron transfer and this compound in turn
phosphorylates ADP to ATP.

2. Conformational coupling hypothesis:

There are many proteins in the wall of inner mitochondrial
membrane; one of them is F0F1, ATPase, which is responsible for the
ATP production. According to this hypothesis the energy liberated
from ETC brings a conformational change in the proteins of the
membrane and is then transferred to FQF1ATPase which thereby also
gets a conformation change and hence becomes unstable. In order to
attain stability it provides energy for ATP synthesis.
3. Chemiosmotic hypothesis:
It states that electron transport pumps H+ from the mitochondrial
matrix across the inner mitochondrial membrane to the outer aqueous
phase, thereby the matrix becomes basic and the outer phase becomes
acidic. Due to this osmotic difference (i.e. more acidic outside and
more basic inside the mitochondrial matrix) the H influx (diffuse) into
the matrix through a pore in the F0F1 ATPase which provides the
energy for the ATP synthesis.
P/O Ratio:
The number of inorganic phosphates esterified per atom of oxygen
consumed is known as P/O ratio. For NADH it is 3 and FADH, it is 2.

Formation and Detoxification of H2O2:

During ETC, O2 accepts four electrons forming two H2O. If by chance
O2 accepts only two electrons, the product formed is H2O2 and if it
accepts only one electron then superoxide radical (:O2~) is formed.
Both these damage the membrane structure by attacking the
unsaturated fatty acids of the membranes.
Superoxide is detoxified as—
2O–2 + 2H + — SUPEROXIDE DISMUTASE → H2O2 + O2
H2O2 is detoxified as—
2H2O2 — CATALASE → 2H2O + O2
Cytochrome-a3:
Cytochrome-a3 is also known as cytochrome oxidase. It has two
molecules of heme with long hydrocarbon side chains. To the other
end of the heme, two copper atoms are attached which can directly
react with oxygen to donate four electrons.
Inhibitors of ETC:
Inhibitors of ETC are those which inhibit or stop the flow of electrons
in the electron transport chain.

Some of the inhibitors of ETC are:

(a) At the first site of ATP formation, rotenone and barbital inhibit the
flow of electrons

(b) At the second site antimycin-A and amytal inhibits the flow of
electrons.

(c) At the third site cyanide (Cn–), carbon monoxide (CO) and H2S gas
inhibit.
Un-couplers of Oxidative Phosphorylation:
Un-couplers are those substances which prevent oxidative
phosphorylation (formation of ATP) though ETC is normally
operating. Due to the effect of un-couplers there is a continuous flow
of electrons but there is no formation of ATP i.e. ETC is not coupled to
the ATP formation, so the energy is dissipated as heat.

Some of the un-couplers are:

1. 2, 4-Dinitrophenol (DNP):
It transfers protons across the mitochondrial membrane thereby
diverting its flow from F0F1 ATPase.
2. Valinomycin:
It transfers K4 ions, disturbing the osmotic pressure.
3. Gramicidin:
It transfers Na+ ions, across the membrane.
All the above three are known as ‘ionophores’ i.e. those which disrupt
the membrane permeability to ions, thereby uncoupling
phosphorylation with ETC.

4. Oligomycin:
It inhibits F0F1ATPase.
5. Atractyloside:
It inhibits adenine nucleotide transport protein of the mitochondrial
membrane which transport ATP in exchange of ADP.
Carbohydrates- definition, structure, types, examples,
functions
What are carbohydrates?
• The carbohydrates are a group of naturally occurring carbonyl compounds
(aldehydes or ketones) that also contain several hydroxyl groups.
• It may also include their derivatives which produce such compounds on
hydrolysis.
• They are the most abundant organic molecules in nature and also referred to
as “saccharides”.
• The carbohydrates which are soluble in water and sweet in taste are called as
“sugars”.
Structure of Carbohydrates
• Carbohydrates consist of carbon, hydrogen, and oxygen.
• The general empirical structure for carbohydrates is (CH2O)n.
• They are organic compounds organized in the form of aldehydes or ketones
with multiple hydroxyl groups coming off the carbon chain.
• The building blocks of all carbohydrates are simple sugars called
monosaccharides.
• A monosaccharide can be a polyhydroxy aldehyde (aldose) or a polyhydroxy
ketone (ketose).
The carbohydrates can be structurally represented in any of the three forms:
• Open chain structure.
• Hemi-acetal structure.
• Haworth structure.
Open chain structure – It is the long straight-chain form of carbohydrates.
Hemi-acetal structure – Here the 1st carbon of the glucose condenses with the -
OH group of the 5th carbon to form a ring structure.
Haworth structure – It is the presence of the pyranose ring structure.
Properties of Carbohydrates
Physical Properties of Carbohydrates
• Stereoisomerism – Compound shaving the same structural formula but they
differ in spatial configuration. Example: Glucose has two isomers with respect
to the penultimate carbon atom. They are D-glucose and L-glucose.
• Optical Activity – It is the rotation of plane-polarized light forming (+) glucose
and (-) glucose.
• Diastereo isomers – It the configurational changes with regard to C2, C3, or C4
in glucose. Example: Mannose, galactose.
• Annomerism – It is the spatial configuration with respect to the first carbon
atom in aldoses and second carbon atom in ketoses.
Chemical Properties of Carbohydrates
• Osazone formation: Osazone are carbohydrate derivatives when sugars are
reacted with an excess of phenylhydrazine. eg. Glucosazone
• Benedict’s test: Reducing sugars when heated in the presence of an alkali gets
converted to powerful reducing species known as enediols. When Benedict’s
reagent solution and reducing sugars are heated together, the solution
changes its color to orange-red/ brick red.
• Oxidation: Monosaccharides are reducing sugars if their carbonyl groups
oxidize to give carboxylic acids. In Benedict’s test, D-glucose is oxidized to D-
gluconic acid thus, glucose is considered a reducing sugar.
• Reduction to alcohols: The C=O groups in open-chain forms of carbohydrates
can be reduced to alcohols by sodium borohydride, NaBH4, or catalytic
hydrogenation (H2, Ni, EtOH/H2O). The products are known as “alditols”.
Properties of Monosaccharides
• Most monosaccharides have a sweet taste (fructose is sweetest; 73% sweeter
than sucrose).
• They are solids at room temperature.
• They are extremely soluble in water: – Despite their high molecular weights,
the presence of large numbers of OH groups make the monosaccharides
much more water-soluble than most molecules of similar MW.
• Glucose can dissolve in minute amounts of water to make a syrup (1 g / 1 ml
H2O).
Classification of Carbohydrates (Types of Carbohydrates)
The simple carbohydrates include single sugars (monosaccharides) and polymers,
oligosaccharides, and polysaccharides.
Monosaccharides
• Simplest group of carbohydrates and often called simple sugars since they
cannot be further hydrolyzed.
• Colorless, crystalline solid which are soluble in water and insoluble in a non-
polar solvent.
• These are compound which possesses a free aldehyde or ketone group.
• The general formula is Cn(H2O)nor CnH2nOn.
• They are classified according to the number of carbon atoms they contain
and also on the basis of the functional group present.
• The monosaccharides thus with 3,4,5,6,7… carbons are called trioses, tetroses,
pentoses, hexoses, heptoses, etc., and also as aldoses or ketoses depending
upon whether they contain aldehyde or ketone group.
• Examples: Glucose, Fructose, Erythrulose, Ribulose.
Oligosaccharides
• Oligosaccharides are compound sugars that yield 2 to 10 molecules of the
same or different monosaccharides on hydrolysis.
• The monosaccharide units are joined by glycosidic linkage.
• Based on the number of monosaccharide units, it is further classified as
disaccharide, trisaccharide, tetrasaccharide etc.
• Oligosaccharides yielding 2 molecules of monosaccharides on hydrolysis is
known as a disaccharide, and the ones yielding 3 or 4 monosaccharides are
known as trisaccharides and tetrasaccharides respectively and so on.
• The general formula of disaccharides is Cn(H2O)n-1and that of trisaccharides is
Cn(H2O)n-2 and so on.
• Examples: Disaccharides include sucrose, lactose, maltose, etc.
• Trisaccharides are Raffinose, Rabinose.
Polysaccharides
• They are also called as “glycans”.
• Polysaccharides contain more than 10 monosaccharide units and can be
hundreds of sugar units in length.
• They yield more than 10 molecules of monosaccharides on hydrolysis.
• Polysaccharides differ from each other in the identity of their recurring
monosaccharide units, in the length of their chains, in the types of bond
linking units and in the degree of branching.
• They are primarily concerned with two important functions ie. Structural
functions and the storage of energy.
• They re further classified depending on the type of molecules produced as a
result of hydrolysis.
• They may be homopolysaccharidese, containing monosaccharides of the same
type or heteropolysaccharides i.e., monosaccharides of different types.
• Examples of Homopolysaccharides are starch, glycogen, cellulose, pectin.
• Heteropolysaccharides are Hyaluronic acid, Chondroitin.
Functions
Carbohydrates are widely distributed molecules in plant and animal tissues. In
plants and arthropods, carbohydrates from the skeletal structures, they also serve
as food reserves in plants and animals. They are important energy source
required for various metabolic activities, the energy is derived by oxidation.
Some of their major functions include:
• Living organisms use carbohydrates as accessible energy to fuel cellular
reactions. They are the most abundant dietary source of energy (4kcal/gram)
for all living beings.
• Carbohydrates along with being the chief energy source, in many animals, are
instant sources of energy. Glucose is broken down by glycolysis/ Kreb’s
cycle to yield ATP.
• Serve as energy stores, fuels, and metabolic intermediates. It is stored as
glycogen in animals and starch in plants.
• Stored carbohydrates act as an energy source instead of proteins.
• They form structural and protective components, like in the cell wall of plants
and microorganisms. Structural elements in the cell walls of bacteria
(peptidoglycan or murein), plants (cellulose) and animals (chitin).
• Carbohydrates are intermediates in the biosynthesis of fats and proteins.
• Carbohydrates aid in the regulation of nerve tissue and is the energy source
for the brain.
• Carbohydrates get associated with lipids and proteins to form surface
antigens, receptor molecules, vitamins, and antibiotics.
• Formation of the structural framework of RNA and DNA (ribonucleic acid and
deoxyribonucleic acid).
• They are linked to many proteins and lipids. Such linked carbohydrates are
important in cell-cell communication and in interactions between cells and
other elements in the cellular environment.
• In animals, they are an important constituent of connective tissues.
• Carbohydrates that are rich in fiber content help to prevent constipation.
• Also, they help in the modulation of the immune system.

ISOMERISM IN CARBOHYDRATES

⇒ Isomers are the compounds having same molecular formula but

different structural formula and this phenomenon are known as
isomerism.
⇒ Isomers are of two types –

• Structural isomers – The isomers having same molecular formula

but different structure are called as structural isomers.
• Stereoisomers – The compounds having same molecular formula
and structure but differs only in the spatial configuration.

⇒ Enantiomers – They are non-superimposed mirror images of each

other. D- and L- isomers are mirror images of each other. When the
hydroxyl group is present on the right side the sugar is D- isomer and if it
is on the left side it is L- isomer. For e.g. D-Glyceraldehyde and L-
Glyceraldehyde.

⇒ Diastereomers – The stereoisomers having the different

configuration at two or more stereocenters are not the mirror images of
each other they are called as diastereomers.
⇒ Optical activity – The substances which rotate the plane polarised
light either towards right or towards left are said to be optically active
substances and the property is known as optical activity. Those
compounds which rotate light towards the right are called as Dextro-
rotatory and the compounds which rotate plane polarised light towards
left are known as Laevo-rotatory.

Reducing and non-reducing sugars

What are Reducing sugars?
• Reducing sugar is a sugar or a carbohydrate molecule with a free aldehyde
group or a free ketone group which causes the molecule to act as a reducing
agent.
• All monosaccharides, along with some disaccharides and polysaccharides, are
reducing sugars.
• In the case of other polysaccharides and disaccharides, the aldehyde and
ketone groups remain bound in the cyclic form.
• Most reducing sugars are sweet in taste. These sugars can be detected by
tests like Benedict’s test and Fehling’s test as they give a positive result to
these tests.
• Examples of reducing sugars include monosaccharides like
galactose, glucose, glyceraldehyde, fructose, ribose, and xylose, disaccharides
like cellobiose, lactose, and maltose, and polymers like glycogen.
What are Non-reducing sugars?
• A non-reducing sugar is a sugar or carbohydrate molecule that doesn’t have a
free aldehyde or ketone group and thus cannot act as a reducing agent.
• Non-reducing sugars have aldehyde and ketone groups, but they are
involved in the cyclic form of the sugar molecule.
• Some disaccharides and all polysaccharides are non-reducing sugars.
• Non-reducing sugars have a less sweet taste than the reducing sugars. These
sugars can also be detected by tests like Benedict’s test and Fehling’s test as
they give a negative result to these tests.
• Examples of non-reducing sugars include disaccharides like sucrose, maltose,
and lactose and polysaccharides like starch and cellulose.
Formation of a glycosidic bond by condensation
• The process of formation of glycosidic bonds in carbohydrates is a
condensation reaction which means that a molecule of water is formed during
the process.
• The condensation reaction is formed between the OH group and the
anomeric carbon of a sugar.
• These glycosidic bonds are formed in a dehydration synthesis reaction.
• When the alcohol attacks the anomeric carbon, the OH group of the carbon is
replaced by the oxygen atom of the alcohol molecule. The OH group of the
carbon and the remaining H atom of the alcohol are released in the form of a
water molecule.
• The glycosylation reaction involves nucleophilic displacement at the anomeric
center. As the reaction takes place at the secondary carbon atom by the
attack of weak nucleophiles (sugar acceptors), it often follows a unimolecular
SN1 mechanism.
• The result of a glycosidic bond is a sugar molecule bound to another
molecule by an ether group.
• The ether bond formed has an oxygen atom bonded to two carbon atoms
which result in a relatively stable structure than with the alcohol group. As a
result, a glycosidic bond results in a more stable structure of the sugar.
Breakage of a glycosidic bond by hydrolysis
• The breakage of a glycosidic bond occurs by the process of hydrolysis by the
addition of a water molecule.
• Hydrolysis of glycosidic bond occurs both in the presence of acid or an alkali.
• The OH group from the water molecule attacks the carbon atom involved in
the glycosidic linkage.
• In acid-catalyzed hydrolysis, the hydrogen atom binds to the oxygen atom of
the ether bond separating the monomeric units.
• In the case of polysaccharides, hydrolysis results in smaller polysaccharides or
disaccharides, or monosaccharides.
• In the living system, hydrolysis of polysaccharides occurs in the presence of a
group of enzymes termed hydrolases that catalyze the hydrolysis process.
Examples of Polysaccharides
1. Starch
Starch is a polysaccharide comprising glucose monomers joined together by
glycosidic linkages. Starch is an organic compound found in all living plants
which is manufactured from the excess glucose produced during photosynthesis.
Starch is the form of reserve food in plants stored in chloroplasts in the form of
granules and storage organs like roots, tuber, stem, and seeds.
Structure
• Starch is a homoglycan composed of a single type of sugar unit, regardless of
the source of the starch.
• A single starch molecule has 300 to 1000 glucose units bound together.
• Most starches are composed of two kinds of polysaccharides, a linear α-(1→4)
linked glucan, called amylose, and an α-(1→4) linked glucan with 4.2 to 5.9%
α-(1→6) branch linkages, called amylopectin.
• The ratio of amylose to amylopectin also varies, depending on the source of
the starch; it ranges from 17 to 70% amylose and a corresponding 83 to 30%
amylopectin.
• α-amylose or simply amylose has a molecular weight range of 10,000 to
50,000, which may be formed in plant cells by the elimination of a molecule of
water from a glycosidic OH group of one α-D-glucose molecule and alcoholic
OH group on carbon 4 of the adjacent α-D-glucose molecule.
• The linkage in amylose is, thus, an α-1, 4-glucoside.
• β-amylose or amylopectin has a high molecular weight range of 50,000 to
1,000,000, thus indicating the presence of 300–5,500 glucose units per
molecule.
• Additional α-1,6-glucoside linkages are found in amylopectin in addition to
the α-1,4-glucoside linkages.
• In plants, starch molecules are arranged in the form of semi-crystalline
granules.
Functions
• Starch is the most common and essential storage form of carbohydrates in
plants.
• It is a major source of energy in a carbohydrate diet where the hydrolysis of
starch yields glucose which is further metabolized to produce energy.
2. Glycogen
Glycogen is a branched polysaccharide that is a major form of glucose in animals
and humans. It is often termed as ‘animal starch’ and is stored in the liver and
muscles of animals.
Structure
• Glycogen is a branched-chain polysaccharide and resembles amylopectin in
its structure.
• Glycogen molecule is composed of glucose subunits that are linked together
by α-1,4 linkages that branch off via α-1,6 linkages every ten glucose
residues.
• These linkages result in a helical polymer structure that exists in the form of
granules in the cytoplasm.
• Glycogen is similar to starch but has more branches and is more compact
than starch.
• Glycogen is synthesized in the body when there is an excess of glucose
produced in the body.
Functions
• The primary function of glycogen is the storage of excess glucose in the body
when the blood glucose level increases.
• Glycogen then breaks down into glucose molecules to provide energy to the
body when the blood glucose level decreases.
• By allowing the formation and hydrolysis, glycogen helps to maintain the
blood glucose level.
• About 6-10% of the weight of the liver is made up of glycogen which is
converted into glucose molecules during fasting.
• Reserved glycogen in the muscle cells serves as a fuel or the supply of ATP
during muscle contraction.
3. Cellulose
Cellulose is the most abundant extracellular structural polysaccharide in plants
and the most abundant of all biomolecules in the biosphere. Cellulose is found in
all land plants but is absent in meat, egg, fish, and milk. It, however, cannot be
metabolized by the human system. Cellulose occurs in the cell walls of plants
where it contributes in a major way to the structure of the organism.
Structure
• The molecular weight of cellulose ranges between 200,000 and 2,000,000,
thus corresponding to 1,250–12,500 glucose residues per molecule.
• It is formed by the glycosidic linkage between the OH group on C1 of one β-
D-glucose molecule and the alcoholic OH group on C4 of the adjacent β-D-
glucose molecule.
• It resembles in structure with amylose except that the glucose units are linked
together by β-1, 4-glucoside linkages.
Functions
• Cellulose is the major structural polysaccharide in plants that forms the
various structure of plant cells, including the cell wall.
• Cellulose has high rigidity and strength that enables the cell to have a solid
structure and shape.
• Cellulose can be degraded into smaller monosaccharides like glucose which
can then be broken down metabolically to produce energy.
• It is also important for the formation of paper and wood.