Bioinorganic chemistry
• role of metals in biology.
• Metalloproteins and their role in biological
processes such as respiration and photosynthesis.
• Bioinorganic chemistry deals with electron-
transfer proteins, substrate bindings and
activation, atom and group transfer chemistry as
well as metal properties in biological chemistry.
• Collection of metal-containing biomolecules in a
cell is called the metallome.
Transporters
• (e.g. the ion pump Na K ATPase), vacuoles,
storage proteins (e.g.ferritin), and small
molecules (e.g.siderophores)
• employed to control metal ions concentration
and bio-availability in living organisms.
Electron transfer proteins
• Metal containing electron transfer protein
1 Iron- sulfur protein
2 Copper protein
3 Cytochrome
• Non-metal electron transporters
1 NAD (Nicotinamide adenine dinucleotide)
2 FAD (Flavin adenine dinucleotide)
Iron–sulfur protein
• Contain iron-sulfur clusters.
• Contain sulfide-linked di, tri and tetra iron centers in
variable oxidation states.
• Iron-sulfur clusters are found in ferredoxins, NADH
dehydrogenase, Hydrogenase, Coenzyme Q-cytochrome c
reductase, succinate-coenzyme Q reductase and
Nitrogenase.
• Iron-sulfur clusters are important for redox reactions.
• In most Fe-S proteins, the terminal ligands on Fe are
thiolate.
Structure
• Fe centers are tetrahedral and the terminal
ligands are thiolato sulfur centers from
cysteinyl residues.
• sulfide groups are either two- or three-
coordinated.
• 1. 2Fe–2S clusters eg (ferrodoxin, Rieske
protein)
• 2. 4Fe–4S clusters eg (aconitase)
• 3. 3Fe–4S clusters
2Fe–2S clusters
• Two iron ions are
bridged by two sulfide
ions and coordinated by
four cysteinyl ligands or
by two cysteines and
two histidines.
4Fe–4S clusters
• Four iron ions and four sulfide ions placed at the vertices of a
cubane-type cluster.
• The Fe centers are further coordinated by cysteinyl ligands.
• 4Fe–4S clusters may bind substrates and are thus classified as
enzyme cofactors. Eg aconitase.
• Clusters in ferrodoxin are subdivided into low-potential and high
potential forrodoxins.
• In high-potential (HiPIP), the cluster shuttles between [2Fe3+,
2Fe2+] (Fe4S42+) and [3Fe3+, Fe2+] (Fe4S43+).
3Fe–4S clusters
• contain [Fe3S4] centres.
• Three sulfide ions bridge two iron ions each,
while the fourth sulfide bridges three iron ions.
• oxidation states may vary from [Fe3S4]+ (all-Fe3+
form) to [Fe3S4]2− (all-Fe2+ form).
Other Fe–S clusters
• In nitrogenase there are the 8Fe and the 7Fe
clusters.
• Carbon monoxide dehydrogenase and [FeFe]-
hydrogenase also feature ubusual Fe-S
clusters.
• In [NiFe] hydrogenase a 6 cysteine-
coordinated [Fe4S3] cluster is found.
Nitrogenase complex
• Nitrogenase complex is made of reductase
and nitrogenase.
Reductase (Fe protein )
• reductase (Fe protein ): is a dimer of identical
subunits which contains one [Fe4S4] cluster.
• It transfer electrons from a reducing agent,
such as ferredoxin or flavodoxin to the
nitrogenase protein.
Nitrogenase (MoFe protein)
• Nitrogenase (MoFe protein): is a
heterotetramer consisting of two α subunits
and two β subunits,
• two iron-sulfur clusters, known as P-clusters,
located at the interface between the α and β
subunits and two FeMo cofactors, within the α
subunits.
• the two P-clusters takes the form of two
[Fe4S3] cubes linked by a central carbon atom.
Each P-cluster is covalently linked to the MoFe
protein by six cysteine residues.
• FeMo cofactor (Fe7MoS9C) consists of two
non-identical clusters: [Fe4S3] and [MoFe3S3],
which are linked by three sulfide ions.
Electrons from the Fe protein enter the MoFe
protein at the P-clusters, which then transfer the
electrons to the FeMo cofactors. Each FeMo
cofactor then acts as a site for nitrogen fixation,
with N2 binding in the central cavity of the cofactor.
Cytochrome
• redox-active proteins containing a heme,
with Fe as cofactor.
• Classified into
cytochromes a
cytochromes b
cytochromes c
cytochromes d
Cytochrome b
• protein found in the
mitochondria of eukaryotic
cells.
• component of respiratory
chain.
• an integral membrane
protein, Consisting of two
hems groups and four
histidine ligands attached
to iron atoms of the two
heme groups.
Cytochrome c
• functions as electron transfer
proteins and catalyses chemical
reactions involving redox
processes.
• have heme C covalently attached
to the peptide backbone via one
or two thioether bonds.
Cytochrome d
• contain heme D as cofactor
• A membrane-bound
hemeprotein, having a heme D.
