I M.

Sc CHEMISTRY UNIT 1 BIOINORGANIC CHEMISTRY

METALLOBIOMOLECULES

DEFINITION

 Biomolecules that contain one or more metallic elements

 These are natural products with complex coordination compounds, the
active sites of which frequently take part in various biochemical processes.
 Electron transport, foreign molecule binding, and catalysis
 Based upon the function of these biomolecules they are classified into three
groups.

[I] Non-protein Part

[a] Chlorophyll

 Radiant solar energy enters the biosphere using magnesium porphyrin

complex through chlorophyll.

RAM KUMAR P ASST PROF OF CHEMISTRY V.O.C.COLLEGE

I M.Sc CHEMISTRY UNIT 1 BIOINORGANIC CHEMISTRY

 The process is also referred as photosynthesis and almost all life processes
depends upon chlorophyll and photosynthesis.
 The energy is stored in the form of carbohydrate and when carbohydrate
molecules breakup into small molecules energy is released and the life
processes use solar energy thus by photosynthesis.

[b] Siderophores

 Siderophores transfer iron into and inside bacterium cells by forming

chelates with iron and transporting the iron into the cells.
 In certain conditions, siderophores release iron at the cell wall and just
iron goes through
 But in other cases, a full complex coordination compound enters the cell
and releases iron as required.

[II] Proteins Part

[1] Electron carriers

[a] Cytochromes

 Cytochromes are heme proteins those act as electron carrier involved in

photosynthesis.
 It consists of a porphyrin ring chelated to iron atom.
 Cytochromes are found in all aerobic forms of life.
 The oxidation state of iron may either II or III and they exist as redox
intermediates in electron transfer reactions.

[b] lron-Sulphur proteins

 Several non-heme iron suiphur proteins are involved in electron transfer.

 They are made up of peptide chains having cysteine moiety
 Cysteine sulphur is coordinated to iron or cluster of iron-sulphur atoms.
Examples : Rubredoxins and Ferridoxins.

[c] Copper blue proteins

RAM KUMAR P ASST PROF OF CHEMISTRY V.O.C.COLLEGE

I M.Sc CHEMISTRY UNIT 1 BIOINORGANIC CHEMISTRY

 They act as electron carriers in photosynthesis and mainly occur in algae,

green leaves and other plants.
 Example: Plastocyanin and Azurin.

[2] Metal storage

[a] Ferritin

 A protein called ferritin may store and release iron in epithelial cells.
 The extra iron can be kept inside the cell in a non-toxic form by attaching
to protein, which is known as apoprotein in mucosal cells.
 Once inside the mucosal cell, iron(Il) is oxidised to iron(III) and
subsequently combined with an apoprotein called ferritin.

[b] Transferrin

 Nearly all the iron released from the mucosal cell enters the portal blood,
mostly in iron (Il) state.
 In the plasma iron (II) is oxidized to iron(III) and then picked upby iron
binding protein transferrin.

[3] Oxygen binding

[a] Hemoglobin and Myoglobin

 The function of oxygen transport and storage in higher animals is provided

by iron-porphyrin complex hemoglobin and myoglobin
 The former transport the oxygen from lungs to site of its use inside the
muscle cell and there the oxygen is transferred to myoglobin for use in
respiration.

[b] Hemerythrin

 A non-heme oxygen binding iron protein used in great variety of marine

worms and phyla of marine invertebrates.
 lt also contains iron(II) which binds oxygen reversibly and when oxidized
to iron(III) (methmerythrin} show no tendency to bind oxygen

RAM KUMAR P ASST PROF OF CHEMISTRY V.O.C.COLLEGE

I M.Sc CHEMISTRY UNIT 1 BIOINORGANIC CHEMISTRY

[c] Hemocyanin

 Hemocyanin contains capper and bind one molecule of oxygen for every
pair of copper (I) ions.
 When oxygen is bound to hemocyanin its colour is blue otherwise
unbound hemocyanin is colourless
 They are found on molluscus and ortropods

[III] Enzyme

 Enzymes are catalyst that enhanced the rates of biochemical reaction from
106 to l012 times that of uncatalysd reactions
 All enzymes are proteins and contain a functional site called the active site
where reactants are converted into products.
 Each enzyme is highly specific, catalyzing one at most a few reactions.
 Enzymes are of interest so inorganic chemists composed of protein
structure (called apoproteins) and a small prosthetic group, which may be
either a simple metal ion or a complex metal ion.
 Zinc is the prosthetic group in carbonic anhydrase and carboxy peptidase.

RAM KUMAR P ASST PROF OF CHEMISTRY V.O.C.COLLEGE