Structure and Function of Oxidation–Reduction Enzymes
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Structure and Function of Oxidation–Reduction Enzymes

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

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eBook - PDF

Structure and Function of Oxidation–Reduction Enzymes

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

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About This Book

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.

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Yes, you can access Structure and Function of Oxidation–Reduction Enzymes by Å. Åkeson,A. Ehrenberg in PDF and/or ePUB format, as well as other popular books in Biological Sciences & Biology. We have over one million books available in our catalogue for you to explore.

Information

Publisher
Pergamon
Year
2014
ISBN
9781483147550
Topic
Biological Sciences
Subtopic
Biology
Index
Biological Sciences

Table of contents

  1. Front Cover
  2. Structure and Function of Oxidation-Reduction Enzymes
  3. Copyright Page
  4. Table of Contents
  5. PREFACE
  6. CHAPTER 1. OPENING ADDRESS
  7. CHAPTER 2. IN MEMORIAM OF OTTO WARBURG
  8. CHAPTER 3. FUNCTIONAL LIMITS OF CYTOCHROME c VARIABILITY
  9. CHAPTER 4. VERTEBRATES AND INSECT HAEMOGLOBINS: A NEW HAEMCOMPLEX
  10. CHAPTER 5. COMMENT ON ARTICLE BY G. BRAUNITZER
  11. CHAPTER 6. THE PRIMARY STRUCTURE OF SOYBEAN LEGHEMOGLOBIN
  12. CHAPTER 7. AMINO-ACID SEQUENCE IN CYTOCHROME c FROM MYXINE GLUTINOSA L.
  13. CHAPTER 8. CHEMICAL SYNTHESIS OF THE CYTOCHROME c MOLECULE
  14. CHAPTER 9. THE PRIMARY STRUCTURE OF HORSE-LIVER ALCOHOL DEHYDROGENASE
  15. CHAPTER 10. TENTATIVE AMINO-ACID SEQUENCE OF BOVINE-LIVER GLUTAMATE DEHYDROGENASE AND CERTAIN PROPERTIES OF THE ENZYME
  16. CHAPTER 11. FERRICYTOCHROME c: II. CHAIN FLEXIBILITY AND A POSSIBLE REDUCTION MECHANISM
  17. CHAPTER 12. THE STRUCTURE OF LACTATE DEHYDROGENASE AT 2.8 Å RESOLUTION
  18. CHAPTER 13. THE STRUCTURE OF HORSE-LIVER ALCOHOL DEHYDROGENASE. III. MOLECULAR STRUCTURE AT 5 Å RESOLUTION
  19. CHAPTER 14. A NEUTRON DIFFRACTION ANALYSIS OF MY0GL0BIN:II. HYDROGEN-DEUTERIUM BONDING IN THE MAIN CHAIN
  20. CHAPTER 15. STRUCTURAL STUDIES ON FLAVIN DERIVATIVES IN DIFFERENT STATES OF OXIDATION
  21. CHAPTER 16. OBSERVATION OF ALLOSTERIC TRANSITION IN HEMOGLOBIN
  22. CHAPTER 17. COMMENT ON ARTICLE BY S. OGAWA AND R. G. SHULMAN
  23. CHAPTER 18. MYOGLOBIN AS A POSSIBLE CARRIER OF OXYGEN
  24. CHAPTER 19. SUBUNIT INTERACTIONS IN ALLOSTERIC CONTROL
  25. CHAPTER 20. SOME PROPERTIES OF SINGLE-CHAIN HEMOGLOBINS
  26. CHAPTER 21. A FLUOROGENIC REAGENT AS A PROBE FOR THE SUBUNIT STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
  27. CHAPTER 22. STRUCTURAL CHANGES OF CYTOCHROME OXIDASE DEPENDENT ON ITS REDOX STATE
  28. CHAPTER 23. CHEMICAL SUBSTITUTION OF HEME PROSTHETIC GROUPS IN HEMOPROTEINS
  29. CHAPTER 24. LOW-TEMPERATURE EPR STUDIES OF THE EFFECTS OF PROTEIN CONFORMATION ON THE SYMMETRY OF HEME IN HIGH-SPIN FERRIHEME PROTEINS
  30. CHAPTER 25. HEME BINDING AND BIOPOLYMER CONFORMATION. THE INTERACTION BETWEEN POLY-α, L-ORNITHINE AND FERRIPROTOPORPHYRIN IX
  31. CHAPTER 26. THE EFFECTS OF VARIOUS OESTROGENS ON THE EOSINOFIL GRANULOCYTES IN THE MOUSE AND RAT ENDOMETRIUM
  32. CHAPTER 27. LOW-SPIN FERRIC FORMS OF HEMOGLOBIN AND OTHER HEME PROTEINS
  33. CHAPTER 28. LIGAND SPECIFICITIES OF INTERACTIONS BETWEEN HAEMOGLOBIN PROTOMERS
  34. CHAPTER 29. KINETICS OF THE REACTIONS OF HEMOGLOBIN WITH LIGANDS, THE REACTION OF HEMOGLOBIN, ISOLATED CHAINS AND INTERMEDIATES WITH ETHYLISOCYANIDE
  35. CHAPTER 30. ROLE OF CYTOCHROMES AND OTHER METALLOPROTEINS IN THE PHOTOSYNTHETIC ELECTRON TRANSPORT
  36. CHAPTER 31. COUPLING AND CONTROL AT THE CYTOCHROME LEVEL OF BACTERIAL PHOTOSYNTHETIC ELECTRON TRANSPORT
  37. CHAPTER 32. THE FUNCTION OF CYTOCHROME c IN MITOCHONDRIAL MEMBRANES
  38. CHAPTER 33. FORMATION OF A STABLE COMPLEX BETWEEN CYTOCHROME b2 AND CYTOCHROME c AND STUDY OF ITS ROLE IN THE OVERALL ELECTRON TRANSFER BY RAPID KINETICS
  39. CHAPTER 34. HIGH-ENERGY FORMS OF CYTOCHROME b
  40. CHAPTER 35. STUDIES OF THE ALKALINE TRANSITIONS OF SOLUBLE FERRICYTOCHROME b5
  41. CHAPTER 36. SUBSTRATE INTERACTION WITH MICROSOMAL CYTOCHROME P-450
  42. CHAPTER 37. THE MANIFOLD OF PEROXIDASE FUNCTION
  43. CHAPTER 38. BIOLOGICAL EFFECTS OF HYPOCHLOROUS ACID FORMED BY "ΜΡΟ''-PEROXIDATION IN THE PRESENCE OF CHLORIDE IONS
  44. CHAPTER 39. NMR DOUBLE-RESONANCE STUDY OF CYTOCHROME c
  45. CHAPTER 40. ALTERNATIVE MOLECULAR FORMS OF ERYTHROCYTE CATALASE
  46. CHAPTER 41. PROTON MAGNETIC RELAXATION ENHANCEMENT OF CYTOCHROME c
  47. CHAPTER 42. KINETIC AND EQUILIBRIUM STUDIES ON THE AUTOREDUCTION OF HORSE-HEART FERRICYTOCHROME c
  48. CHAPTER 43. PEROXIDASE ACTIVITY OF HAEM c AND HAEM e DISULPHONE
  49. CHAPTER 44. FLAVIN-DEPENDENT SUBSTRATE DEHYDR0GENATI0N: MODEL STUDIES AND MECHANISMS
  50. CHAPTER 45. EPR AND ENDOR STUDIES ON FLAVOPROTEIN RADICALS
  51. CHAPTER 46. PROTON RELAXATION RATE ENHANCEMENT WITH FREE AND PROTEIN-BOUND FLAVIN RADICALS
  52. CHAPTER 47. THERMODYNAMICS AND KINETICS OF THE INTRAMOLECULAR COMPLEX IN FLAVIN-ADENINE DINUCLEOTIDE
  53. CHAPTER 48. D-AMINO ACID OXIDASE
  54. CHAPTER 49. RIBOFLAVIN FLAVOPROTEIN FROM EGG-YOLK
  55. CHAPTER 50. ON THE KINETICS OF GLUTATHIONE REDUCTASE
  56. CHAPTER 51. DT DIAPHORASE — REACTION MECHANISM AND METABOLIC FUNCTION
  57. CHAPTER 52. THE ROLE OF FLAVINS IN HYDROXYLASE REACTIONS
  58. CHAPTER 53. STUDIES ON THE MECHANISM OF SALICYLATE HYDROXYLASE
  59. CHAPTER 54. STRUCTURE AND REACTION MECHANISM OF LIPOAMIDE DEHYDROGENASE FROM PIG HEART
  60. CHAPTER 55. KINETIC AND REDOX PROPERTIES OF FLAVOPROTEINS IN MITOCHONDRIA
  61. CHAPTER 56. THE COVALENTLY BOUND FLAVIN ACTIVE CENTER OF SUCCINATE DEHYDROGENASE
  62. CHAPTER 57. STUDIES ON THE CATALYSIS OF HYDROGEN EXCHANGE BETWEEN (S)-(-)-CHLOROSUCCINATE AND WATER BY SUCCINIC DEHYDROGENASE
  63. CHAPTER 58. CHEMICAL ACTIVATION OF RECONSTITUTIVELY INACTIVE SUCCINATE DEHYDROGENASE
  64. CHAPTER 59. STUDIES ON THE COPPER IONS IN RHUS-LACCASE
  65. CHAPTER 60. STRUCTURE OF MICROBIAL IRON TRANSPORT COMPOUNDS
  66. CHAPTER 61. A RAPID METHOD FOR STUDYING THE BINDING OF SMALL IONS AND MOLECULES TO MACROMOLECULES: CONTINUOUS ENTHALPYTITRATION
  67. CHAPTER 62. KINETICS OF ENZYME-SUBSTRATE REACTIONS IN SINGLE LIVING CELLS
  68. CHAPTER 63. RELATIONSHIP OF ELECTRON TRANSPORT ENZYMES TO MICROSOMAL MEMBRANES
  69. CHAPTER 64. FORMYLGLYCINAMIDE RIBONUCLEOTIDE AMIDOTRANSFERASE: A BRIEF REVIEW
  70. CHAPTER 65. THE ORDER OF ADDITION OF SUBSTRATES TO AMINO ACID: tRNA LIGASES
  71. CHAPTER 66. EXCITATION TRANSFER BETWEEN THE SUBUNITS OF LIVER ALCOHOL DEHYDROGENASE
  72. CHAPTER 67. 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
  73. CHAPTER 68. CARBOXYMETHYL-LIVER ALCOHOL DEHYDROGENASE AND BINDING STUDIES WITH IODOACETATE AND PYRIDOXAL PHOSPHATE
  74. CHAPTER 69. CARBOXYMETHYL-LIVER ALCOHOL DEHYDROGENASE AND BINDING STUDIES WITH IODOACETATE AND PYRIDOXAL PHOSPHATE
  75. CHAPTER 70. BINDING OF COENZYME TO NATIVE AND ZINC-FREE HORSE-LIVER ALCOHOL DEHYDROGENASE
  76. CHAPTER 71. TERNARY COMPLEXES OF HORSE-LIVER ALCOHOL DEHYDROGENASE, OXIDIZED COENZYME AND FATTY-ACID AMIDES
  77. CHAPTER 72. RAT-LIVER ALCOHOL DEHYDROGENASE (RLADH)
  78. CHAPTER 73. GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
  79. CHAPTER 74. COMMENT ON ARTICLE BY J. IEUAN HARRIS
  80. CHAPTER 75. SOLVENT EFFECTS ON NADH FLUORESCENCE IN SOLUTION AND IN COMPLEXES WITH ALCOHOL DEHYDROGENASE AND HYDROXYSTEROID DEHYDROGENASE
  81. CHAPTER 76. INHIBITION OF LADH BY BERBERINE AND SOME RELATED ALKALOIDS
  82. CHAPTER 77. TRANSFER OF HYDROGEN FROM ETHANOL TO STEROIDS DURING ETHANOL METABOLISM IN THE RAT
  83. CHAPTER 78. RESULTS AND DISCUSSION
  84. CHAPTER 79. STUDIES ON THE REGULATION OF ETHANOL OXIDATION IN MAN
  85. CHAPTER 80. PHYSICO-CHEMICAL STUDIES OF GLUTAMATE DEHYDROGENASE IN SOLUTION
  86. CHAPTER 81. COMPLEXES OF PYRIDINE NUCLEOTIDES AND THEIR FUNCTION
  87. CHAPTER 82. RAT-LIVER LACTATE DEHYDROGENASE-COENZYME (OR ANALOG) COMPLEXES: DIFFERENCE SPECTROPHOTOMETRIC STUDY
  88. CHAPTER 83. IS THERE A GLYCOLYTIC PARTICLE?
  89. CHAPTER 84. NEGATIVE INTERACTIONS IN THE GLUTAMATE DEHYDROGENASE REACTION
  90. CHAPTER 85. GENERAL RELATIONSHIPS BETWEEN DALZIEL COEFFICIENTS AND VELOCITY CONSTANTS IN THE RANDOM-ORDER TWO-SUBSTRATE MECHANISM
  91. CHAPTER 86. STUDIES OF DEHYDROGENASE MECHANISMS USING ADP-TETRAMETHYLPIPERIDINE-1-OXYL (ADP-R·), A PARAMAGNETIC ANALOG OF NAD
  92. CHAPTER 87. THE ANALYSIS OF TRANSIENTS IN NAD+-LINKED DEHYDROGENASESE
  93. CHAPTER 88. MATERIALS AND METHODS
  94. CHAPTER 89. COMMENT ON ARTICLE BY J. D. SHORE and H. GUTFREUND
  95. CHAPTER 90. CONCLUDING REMARKS
  96. INDEX