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    METALLOBIMOLECULES

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    RAM KUMAR
    This document discusses metallobiomolecules, which are biomolecules that contain metallic elements. They are classified into three groups: non-protein parts, proteins for electron transport, and enzymes. Non-protein parts include chlorophyll, which uses magnesium to facilitate photosynthesis, and siderophores, which transport iron into bacterial cells. Protein parts involve electron carriers like cytochromes, iron-sulfur proteins, and copper proteins. They also include ferritin and transferrin for metal storage and hemoglobin, myoglobin, and hemerythrin for oxygen binding. Enzymes are proteins that catalyze biochemical reactions and some contain prosthetic metal ion groups like zinc.

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    METALLOBIMOLECULES

    Uploaded by

    RAM KUMAR
    72 views4 pages
    This document discusses metallobiomolecules, which are biomolecules that contain metallic elements. They are classified into three groups: non-protein parts, proteins for electron transport, and enzymes. Non-protein parts include chlorophyll, which uses magnesium to facilitate photosynthesis, and siderophores, which transport iron into bacterial cells. Protein parts involve electron carriers like cytochromes, iron-sulfur proteins, and copper proteins. They also include ferritin and transferrin for metal storage and hemoglobin, myoglobin, and hemerythrin for oxygen binding. Enzymes are proteins that catalyze biochemical reactions and some contain prosthetic metal ion groups like zinc.

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    This document discusses metallobiomolecules, which are biomolecules that contain metallic elements. They are classified into three groups: non-protein parts, proteins for electron transport, and enzymes. Non-protein parts include chlorophyll, which uses magnesium to facilitate photosynthesis, and siderophores, which transport iron into bacterial cells. Protein parts involve electron carriers like cytochromes, iron-sulfur proteins, and copper proteins. They also include ferritin and transferrin for metal storage and hemoglobin, myoglobin, and hemerythrin for oxygen binding. Enzymes are proteins that catalyze biochemical reactions and some contain prosthetic metal ion groups like zinc.

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    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    72 views4 pages

    METALLOBIMOLECULES

    Uploaded by

    RAM KUMAR
    This document discusses metallobiomolecules, which are biomolecules that contain metallic elements. They are classified into three groups: non-protein parts, proteins for electron transport, and enzymes. Non-protein parts include chlorophyll, which uses magnesium to facilitate photosynthesis, and siderophores, which transport iron into bacterial cells. Protein parts involve electron carriers like cytochromes, iron-sulfur proteins, and copper proteins. They also include ferritin and transferrin for metal storage and hemoglobin, myoglobin, and hemerythrin for oxygen binding. Enzymes are proteins that catalyze biochemical reactions and some contain prosthetic metal ion groups like zinc.

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    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

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