Overview

Approximately one third of the mass of a mammalian red blood cell is hemo- globin. Its major function is to bind oxygen at the partial pressure prevailing in the lungs and to release it to the tissues where the partial pressure is lower. The process whereby hemoglobin performs this essential physiological role is characterized by a cooperative interaction among its constituent subunits. A great deal of research effort has been devoted to this interaction, going back at least as far as the fitst decade of this century. Moreover, cooperativity in hemo- globin is probably not unique; it may well be one instance of a general class of interactions that occur in biological molecules. Certain enzymes with a variety of regulatory and catalytic functions, for example, contain several sites which interact in a highly specific manner such that the affinity of a given site for the substrate is markedly influenced by the state of binding at the other sites. But whereas we know very little of the structure of most enzymes of this type, hemo- globin is one of a very small number of biological molecules whose immensely intricate machinery has been revealed to us. We owe this insight to the group under the leadership of M. F. PERUTZ in Cambridge, England, whose research over a period of several decades culminated in a detailed description of the three- dimensional structure.

Full Product Details

Author:   M. Weissbluth
Publisher:   Springer-Verlag Berlin and Heidelberg GmbH & Co. KG
Imprint:   Springer-Verlag Berlin and Heidelberg GmbH & Co. K
Volume:   15
Weight:   0.550kg
ISBN:  

9783540065821

ISBN 10:   3540065822
Pages:   184
Publication Date:   10 June 1974
Audience:   Professional and scholarly ,  Professional & Vocational
Format:   Hardback
Publisher's Status:   Out of Print
Availability:   Out of stock  

Table of Contents

I Amino Acids, Peptides and Proteins.- 1.1 Amino Acids.- 1.2 Peptides.- 1.3 Proteins.- II Hemoglobin.- 2.1 Primary Structure.- 2.2 Spin States.- 2.3 Heme.- 2.4 Secondary and Tertiary Structure.- 2.5 Quaternary Structure.- 2.6 Dissociated Hemoglobin.- III Oxygenation Characteristics.- 3.1 Equilibrium Curves.- 3.2 Quantitative Description.- 3.3 The Bohr Effect.- 3.4 Thermodynamic and Kinetic Properties.- IV Approaches to Cooperativity.- 4.1 The Monod-Wyman-Changeux (MWC) Model.- 4.2 The Koshland-Nemethy-Filmer (KNF) Model.- 4.3 Stereochemical Theory.- 4.4 Magnetic Resonance.- 4.5 Discussion.- V Electronic States of Iron.- 5.1 Free Ions.- 5.2 Cubic Symmetry.- 5.2.1 Symmetry Elements.- 5.2.2 Basis Functions.- 5.2.3 Coupling Coefficients.- 5.2.4 Crystal Field Potential.- 5.3 Tetragonal and Rhombic Symmetries.- 5.4 One-Electron Energies.- 5.5 Multielectron Configurations.- 5.6 Kramers Theorem.- 5.7 The Jahn-Teller Effect.- 5.8 Molecular Orbitals.- VI Magnetic Properties.- 6.1 General Features.- 6.1.1 Electron Spin Resonance.- 6.1.2 Paramagnetic Susceptibility.- 6.2 Electron Spin Resonance of Low-Spin Ferrihemoglobin.- 6.3 Electron Spin Resonance of High-Spin Ferrihemoglobin.- 6.3.1 Spin-Orbit Coupling.- 6.3.2 Spin Hamiltonian.- 6.3.3 Interaction with a Magnetic Field.- 6.4 Paramagnetic Susceptibility.- 6.4.1 Low-Spin Ferrihemoglobin.- 6.4.2 High-Spin Ferrihemoglobin.- 6.4.3 Ferrohemoglobin.- 6.5 Discussion.- VII Molecular Orbitals and Optical Spectra.- 7.1 Computational Method.- 7.1.1 Extended Huckel Method with Self-Consistent Charge (EH-SCC).- 7.1.2 Symmetry Considerations.- 7.2 Results of Molecular Orbital Calculations.- 7.3 Optical Spectra.- VIII Mossbauer Spectroscopy.- 8.1 General Features.- 8.1.1 Isomer Shift.- 8.1.2 Quadrupole Splitting.- 8.1.3 Magnetic Hyperfine Interactions.- 8.2 Mossbauer Spectra of Hemoglobin.- 8.3 Theoretical Interpretation and Discussion.- 8.3.1 Quadrupole Splitting.- 8.3.2 Magnetic Hyperfine Interaction.- IX Further Aspects.- 9.1 Diamagnetism of Oxyhemoglobin.- 9.2 The Jahn-Teller Effect and Cooperativity in Hemoglobin.- References.

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