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    Bioinorganic Chemistry

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    Balqis Musa
    This document summarizes key aspects of bioinorganic chemistry, focusing on porphyrins and hemoglobin. It notes that porphyrins have a square planar geometry that can bind metals. Hemoglobin and myoglobin transport and store oxygen in blood and muscles using heme groups consisting of an iron protoporphyrin complex. Hemoglobin is a tetramer that can reversibly bind oxygen to the sixth coordination site of its iron centers. Binding causes structural changes and cooperativity that facilitates oxygen transport and delivery to tissues.

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    Bioinorganic Chemistry

    Uploaded by

    Balqis Musa
    210 views11 pages
    This document summarizes key aspects of bioinorganic chemistry, focusing on porphyrins and hemoglobin. It notes that porphyrins have a square planar geometry that can bind metals. Hemoglobin and myoglobin transport and store oxygen in blood and muscles using heme groups consisting of an iron protoporphyrin complex. Hemoglobin is a tetramer that can reversibly bind oxygen to the sixth coordination site of its iron centers. Binding causes structural changes and cooperativity that facilitates oxygen transport and delivery to tissues.

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    Bioinorganic

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    This document summarizes key aspects of bioinorganic chemistry, focusing on porphyrins and hemoglobin. It notes that porphyrins have a square planar geometry that can bind metals. Hemoglobin and myoglobin transport and store oxygen in blood and muscles using heme groups consisting of an iron protoporphyrin complex. Hemoglobin is a tetramer that can reversibly bind oxygen to the sixth coordination site of its iron centers. Binding causes structural changes and cooperativity that facilitates oxygen transport and delivery to tissues.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    210 views11 pages

    Bioinorganic Chemistry

    Uploaded by

    Balqis Musa
    This document summarizes key aspects of bioinorganic chemistry, focusing on porphyrins and hemoglobin. It notes that porphyrins have a square planar geometry that can bind metals. Hemoglobin and myoglobin transport and store oxygen in blood and muscles using heme groups consisting of an iron protoporphyrin complex. Hemoglobin is a tetramer that can reversibly bind oxygen to the sixth coordination site of its iron centers. Binding causes structural changes and cooperativity that facilitates oxygen transport and delivery to tissues.

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    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    of 11

    Bioinorganic Chemistry

    Chapter 16

    Bioinorganic Chemistry
    Only a few representative examples will be
    presented for these bioinorganic compounds
    and their actions.
    Table 16-1 (mammalian biochemistry)
    Examine the importance of iron.

    A relatively new area of study for bioinorganic


    molecules is the incorporation of MO
    calculations.

    Porphyrins and Related Complexes


    in Bioinorganic Molecules
    A porphine ring has a square planar geometry with a
    pocket in the center.
    Examine Fig. 16-1.

    A metalloporphyrin complex can result by


    incorporating a metal atom into the pocket (look at
    heme from Rasmol).
    Axial sites are available for other ligands.

    Structure, specificity, and reactivity are changed by


    differing the side chains, metal ions, and surrounding
    species.

    Hemoglobin and Myoglobin


    Oxygen transfer and storage agents in the
    blood and muscle tissue.
    Hemoglobin transports oxygen (O2) from the
    lungs/gills to tissues and muscles.
    Myoglobin stores oxygen (O2) in the muscles
    and tissues.
    Oxygen commonly transfers from the hemoglobin
    to the myoglobin for later use.

    Hemoglobin
    Made up of four globin protein subunits ( and ).
    Each protein partially encloses a heme group.

    Each heme group is in a porphyrin pocket.


    One axial position of the iron is bound to an imidazole
    nitrogen from the protein.
    One axial position is available/vacant or has H2O bound
    to it.
    Dissolved O2 can bind reversibly to this axial position.

    http://www.umass.edu/microbio/chime/hemoglob/

    Hemoglobin
    In hemoglobin, the Fe(II) does not become
    oxidized to Fe(III) or Fe(IV).
    Occurs readily in simpler systems (see Figure on the
    next page).

    There needs to be reversible binding of the O2


    without oxidation. A free heme also oxidizes in
    an aqueous environment.
    Why doesnt oxidation occur in hemoglobin by O2 or
    H2O?

    Hemoglobin (Figures)

    Hemoglobin
    In nonoxygenated hemoglobin, the Fe(II) is about
    70 pm out of the plane of the porphyrin nitrogens
    (show with Chime).
    Bonding O2 or CO in the sixth position causes the
    iron to be come planar.
    Fe(II) becomes diamagnetic

    Oxygen bonds at an angle of ~130 degrees (show


    with Chime).
    Explain these structural changes upon bonding.

    Hemoglobin
    There is a considerable amount of
    backbonding from the metal to the O2.
    Can be described as Fe(III)-O2-

    Why is the O2 bent? The energy changes


    very little with this angle.
    suggestions

    Hemoglobin
    Cooperativity
    The function of hemoglobin is to bind O 2 at high oxygen
    pressure and carry it through the blood to needed areas
    (and myoglobin for storage).
    Hb + 4O2 Hb(O2)4
    Hb(O2)4 + 4Mb 4Mb(O2) + Hb

    As one iron binds an oxygen molecule in Hb, the


    molecular shape changes to make binding of
    additional oxygen molecules easier. In a similar
    fashion, initial removal of oxygen triggers the release
    of the remaining oxygens.

    Hemoglobin
    At low partial pressures of
    O2, Mb has a much greater
    affinity for O2.
    K Mb

    [Mb(O 2 )]
    [Mb][O 2 ]

    K Hb

    [Hb(O 2 ) 4 ]
    [Hb][O 2 ]2.8

    The Bohr effect.


    Increased acidity favors the
    release of O2 from Hb(O2)4

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