Structure and Function of Oxidation–Reduction Enzymes

Structure and Function of Oxidation–Reduction Enzymes

Proceedings of the Wenner-Gren Symposium Held at the Wenner-Gren Center, Stockholm, 23–27 August, 1970

1st Edition - January 1, 1972

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  • Editors: Å. Åkeson, A. Ehrenberg
  • eBook ISBN: 9781483147550

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Description

Structure and Function of Oxidation–Reduction Enzymes is a collection of papers presented at the Wenner-Gren Symposium held at the Wenner-Gren Center, Stockholm on August 23-27, 1970. It provides important understanding of the structure and function of oxidation-reduction enzymes: iron, flavin, and nicotinamide enzymes. This book discusses the functional differences among varying structures such cytochrome c, haemoglobins, dehydrogenases, flavins, oestrogens, and peroxidases. It concludes by presenting future expectations, including some questions that need to be addressed. This volume will be of great value to those interested in the present-day research on oxidation-reduction enzymes.

Table of Contents


  • Preface

    Opening Address

    In Memoriam of Otto Warburg

    Functional Limits of Cytochrome c Variability

    Vertebrates and Insect Haemoglobins: A New Haemcomplex

    Comment on Article by G. Braunitzer

    The Primary Structure of Soybean Leghemoglobin

    Amino-Acid Sequence in Cytochrome c from Myxine glutinosa L

    Chemical Synthesis of the Cytochrome c Molecule

    The Primary Structure of Horse-Liver Alcohol Dehydrogenase

    Tentative Amino-acid Sequence of Bovine-Liver Glutamate Dehydrogenase and Certain Properties of the Enzyme

    Ferricytochrome c: II. Chain Flexibility and a Possible Reduction Mechanism

    The Structure of Lactate Dehydrogenase at 2.8 Å Resolution

    The Structure of Horse-Liver Alcohol Dehydrogenase. III. Molecular Structure at 5 Å Resolution

    A Neutron Diffraction Analysis of Myoglobin: II. Hydrogen-Deuterium Bonding in the Main Chain

    Structural Studies on Flavin Derivatives in Different States of Oxidation

    Observation of Allosteric Transition in Hemoglobin

    Comment on Article by S. Ogawa and R. G. Shulman

    Myoglobin as a Possible Carrier of Oxygen

    Subunit Interactions in Allosteric Control

    Some Properties of Single-Chain Hemoglobins

    A Fluorogenic Reagent as a Probe for the Subunit Structure of Glyceraldehyde-3- phosphate Dehydrogenase

    Structural Changes of Cytochrome Oxidase Dependent on Its Redox State

    Chemical Substitution of Heme Prosthetic Groups in Hemoproteins

    Low-Temperature EPR Studies of the Effects of Protein Conformation on the Symmetry of Heme in High-Spin Ferriheme Proteins

    Heme Binding and Biopolymer Conformation. The Interaction between Poly-α, L-Ornithine and Ferriprotoporphyrin IX

    The Effects of Various Oestrogens on the Eosinofil Granulocytes in the Mouse and Rat Endometrium

    Low-Spin Ferric Forms of Hemoglobin and Other Heme Proteins

    Ligand Specificities of Interactions between Haemoglobin Protomers

    Kinetics of the Reactions of Hemoglobin with Ligands. The Reaction of Hemoglobin, Isolated Chains and Intermediates with Ethylisocyanide

    Role of Cytochromes and Other Metalloproteins in the Photosynthetic Electron Transport

    Coupling and Control at the Cytochrome Level of Bacterial Photosynthetic Electron Transport

    The Function of Cytochrome c in Mitochondrial Membranes

    Formation of a Stable Complex between Cytochrome b2 and Cytochrome c and Study of Its Role in the Overall Electron Transfer by Rapid Kinetics

    High-energy Forms of Cytochrome b

    Studies of the Alkaline Transitions of Soluble Ferricytochrome b5

    Substrate Interaction with Microsomal Cytochrome P-450

    The Manifold of Peroxidase Function

    Biological Effects of Hypochlorous Acid formed by "MPO"-peroxidation in the Presence of Chloride Ions

    NMR Double-Resonance Study of Cytochrome c

    Alternative Molecular Forms of Erythrocyte Catalase

    Proton Magnetic Relaxation Enhancement of Cytochrome c

    Kinetic and Equilibrium Studies on the Autoreduction of Horse-heart Ferricytochrome c

    Peroxidase Activity of Haem c and Haem c Disulphone

    Flavin-Dependent Substrate Dehydrogenation : Model Studies and Mechanisms

    EPR and ENDOR Studies on Flavoprotein Radicals

    Proton Relaxation Rate Enhancement with Free and Protein-bound Flavin Radicals

    Thermodynamics and Kinetics of the Intramolecular Complex in Flavin-Adenine Dinucleotide

    D-Amino Acid Oxidase

    Riboflavin Flavoprotein from Egg-Yolk

    On the Kinetics of Glutathione Reductase

    DT Diaphorase—Reaction Mechanism and Metabolic Function

    The Role of Flavins in Hydroxylase Reactions

    Studies on the Mechanism of Salicylate Hydroxylase

    Structure and Reaction Mechanism of Lipoamide Dehydrogenase from Pig Heart

    Kinetic and Redox Properties of Flavoproteins in Mitochondria

    The Covalently Bound Flavin Active Center of Succinate Dehydrogenase

    Studies on the Catalysis of Hydrogen Exchange between (S')-(—)-Chlorosuccinate and Water by Succinic Dehydrogenase

    Chemical Activation of Reconstitutively Inactive Succinate Dehydrogenase

    Studies on the Copper Ions in Rhus-laccase

    Structure of Microbial Iron Transport Compounds

    A Rapid Method for Studying the Binding of Small Ions and Molecules to Macromolecules: Continuous Enthalpy Titration

    Kinetics of Enzyme-Substrate Reactions in Single Living Cells

    Relationship of Electron Transport Enzymes to Microsomal Membranes

    Formylglycinamide Ribonucleotide Amidotransferase: A Brief Review

    The Order of Addition of Substrates to Amino Acid: tRNA Ligases

    Excitation Transfer between the Subunits of Liver Alcohol Dehydrogenase

    The Use of Chloride Ion as Reporter Group for Changes in Protein Conformation. A 35C1 NMR Study of the Binding of Coenzyme and Inhibitors to Horse-liver Alcohol Dehydrogenase

    Carboxymethyl-Liver Alcohol Dehydrogenase and Binding Studies with Iodoacetate and Pyridoxal Phosphate

    Binding of Coenzyme to Native and Zinc-free Horse-liver Alcohol Dehydrogenase

    Ternary Complexes of Horse-liver Alcohol Dehydrogenase, Oxidized Coenzyme and Fatty-Acid Amides

    Rat-Liver Alcohol Dehydrogenase (RLADH)

    Glyceraldehyde 3-Phosphate Dehydrogenase

    Solvent Effects on NADH Fluorescence in Solution and in Complexes with Alcohol Dehydrogenase and Hydroxysteroid Dehydrogenase

    Inhibition of LADH by Berberine and Some Related Alkaloids

    Transfer of Hydrogen from Ethanol to Steroids during Ethanol Metabolism in the Rat

    Studies on the Regulation of Ethanol Oxidation in Man

    Physico-Chemical Studies of Glutamate Dehydrogenase in Solution

    Complexes of Pyridine Nucleotides and Their Function

    Rat-liver Lactate Dehydrogenase-Coenzyme (or Analog) Complexes: Difference Spectrophotometric Study

    Is there a Glycolytic Particle?

    Negative Interactions in the Glutamate Dehydrogenase Reaction

    General Relationships between Dalziel Coefficients and Velocity Constants in the Random-order Two-substrate Mechanism

    Studies of Dehydrogenase Mechanisms using ADP-Tetramethylpiperidine-1-oxyl (ADP-R—P), a Paramagnetic Analog of NAD

    The Analysis of Transients in NAD+-linked Dehydrogenases

    Comment on Article by J. D. Shore and H. Gutfreund

    Concluding Remarks

    Index

Product details

  • No. of pages: 790
  • Language: English
  • Copyright: © Pergamon 1972
  • Published: January 1, 1972
  • Imprint: Pergamon
  • eBook ISBN: 9781483147550

About the Editors

Å. Åkeson

A. Ehrenberg

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