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    Bioinorganic Chemistry

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    Amit Patra
    This lecture discusses metalloproteins and oxygen transport. It covers the classification of biomolecules and enzymes. Hemoglobin is used to illustrate metalloprotein structure, showing it contains four heme groups and four polypeptide chains. Oxygen binding in hemoglobin involves the deoxy and oxy states shifting the iron from high to low spin. The Perutz mechanism describes hemoglobin shifting between tense (T) and relaxed (R) states during oxygen binding and unbinding in a concerted fashion. The Bohr effect relates hemoglobin's oxygen affinity to pH levels. Other metalloproteins discussed include myoglobin and mechanisms of metalloenzymes such as carbonic anhydrase.

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    Bioinorganic Chemistry

    Uploaded by

    Amit Patra
    43 views53 pages
    This lecture discusses metalloproteins and oxygen transport. It covers the classification of biomolecules and enzymes. Hemoglobin is used to illustrate metalloprotein structure, showing it contains four heme groups and four polypeptide chains. Oxygen binding in hemoglobin involves the deoxy and oxy states shifting the iron from high to low spin. The Perutz mechanism describes hemoglobin shifting between tense (T) and relaxed (R) states during oxygen binding and unbinding in a concerted fashion. The Bohr effect relates hemoglobin's oxygen affinity to pH levels. Other metalloproteins discussed include myoglobin and mechanisms of metalloenzymes such as carbonic anhydrase.

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    Lecture 21

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    This lecture discusses metalloproteins and oxygen transport. It covers the classification of biomolecules and enzymes. Hemoglobin is used to illustrate metalloprotein structure, showing it contains four heme groups and four polypeptide chains. Oxygen binding in hemoglobin involves the deoxy and oxy states shifting the iron from high to low spin. The Perutz mechanism describes hemoglobin shifting between tense (T) and relaxed (R) states during oxygen binding and unbinding in a concerted fashion. The Bohr effect relates hemoglobin's oxygen affinity to pH levels. Other metalloproteins discussed include myoglobin and mechanisms of metalloenzymes such as carbonic anhydrase.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    43 views53 pages

    Bioinorganic Chemistry

    Uploaded by

    Amit Patra
    This lecture discusses metalloproteins and oxygen transport. It covers the classification of biomolecules and enzymes. Hemoglobin is used to illustrate metalloprotein structure, showing it contains four heme groups and four polypeptide chains. Oxygen binding in hemoglobin involves the deoxy and oxy states shifting the iron from high to low spin. The Perutz mechanism describes hemoglobin shifting between tense (T) and relaxed (R) states during oxygen binding and unbinding in a concerted fashion. The Bohr effect relates hemoglobin's oxygen affinity to pH levels. Other metalloproteins discussed include myoglobin and mechanisms of metalloenzymes such as carbonic anhydrase.

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    Lecture 21

    Bioinorganic Chemistry

    Classification of Biomolecules

    Classification of Enzymes

    Transport and Storage Proteins

    Metalloproteins Structure of Heme and Hemoglobin (Hb)


    Hb Structure of Heme
    4 x Heme group + 4 x Polypeptide chain

    The Myogenic Control of Heartbeat

    Bundle of His

    Purkinje fibre

    O2 Binding in Hemoglobin

    Structural Variation of Hb during O2 Binding

    DeoxyHb
    Fe(II) (0.78 ), 5 coordinate coordinate Domed, Nonplanar 0.6 above the ring High Spin, Paramagnetic

    OxyHb
    Fe(III) (0.61 ), 6 Planar, O2 ion Fit into the ring Low Spin, Diamagnetic

    Perutz Mechanism
    Very fast 1. Fe(II) in T state site above heme Fe(II) binds to O2 Fe(III) pulled down into heme (R state) 2. Fe(III) pulls down His F8 F helix tilts

    Animation

    Perutz Mechanism
    3. 4. Shift of tertiary structure causes shift of quaternary structure (rotate) a2b1 and a1b2 interface residues realign C-terminal residues break ionic interactions which stabilize T state As R state forms from T state, it adopts ideal conformation for next O2 binding All binding sites are altered, not just the one binding the O2

    Perutz Mechanism: Pictorial Representation

    DEOXYGENATED VS. OXYGENATED HEMOGLOBIN (CONT.)


    The transition of hemoglobin from the T- to the R-state is not well-defined Best explained as a combination of a sequential and a concerted model

    It is unknown whether the a and b subunits differ in O2 affinity and which subunit binds to (or releases) O2 first.

    Bohr Effect
    Conformational change will be accompanied by change in IFs
    Change in charge

    Also, H+ and O2 compete for binding to Hb

    Relate pH to affinity
    Bohr effect O2 affinity increases as pH increases

    Animation (YO2 = q)

    Formation of Hematin and Role of Protein in Hb

    Structure of Myoglobin (Hb)

    Structural Variation of Hb during O2 Binding

    DEOXYGENATED VS. OXYGENATED HEMOGLOBIN (CONT.)


    The transition of hemoglobin from the T- to the R-state is not well-defined Best explained as a combination of a sequential and a concerted model

    It is unknown whether the a and b subunits differ in O2 affinity and which subunit binds to (or releases) O2 first.

    Cooperative interaction

    Hill Constant

    Hill Constant

    INTERACTIONS WITH O2
    * Can bind up to 4 O2 molecules * Binding of O2 is cooperative: the binding of 1 O2 influences the binding of another

    Mb model for O2 bonding

    O2 bonding in Hemocyanin (Hc)

    O2 bonding in Hemerythrin (Hr)

    O2 bonding Mechanism in Hemerythrin (Hr)

    Metalloenzymes e.g. Carbonic Anhydrase

    Mechanism of Carbonic Anhydrase

    Carboxy Peptidase

    Mechanism of Carboxy Peptidase

    Metals in Medicine
    Vitamin B12

    Vitamin B12 Co-enzyme

    Cis-Platin

    Cis-Platin Binding to DNA

    Crystal Structure of Cis-Platin Binding to DNA

    Other Drugs Used in Anticancer Therapy

    Backup Slides

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