Iron and Copper Proteins

1. Front Matter

   Pages i-xi

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2. Iron-Sulfur Proteins

   1. Structure and Function of Chloroplast-Type Ferredoxins

      • Hiroshi Matsubara, Keishiro Wada, Ryuichi Masaki

      Pages 1-15

   2. Structural Investigations of the Environment of the Iron-Sulfur Cluster of the 2-Iron Ferredoxins

      • J. Drum, K. T. Yasunobu, R. E. Cramer

      Pages 16-35

   3. Studies on Bovine Adrenal Ferredoxin

      • S. Takemori, K. Suhara, M. Katagiri

      Pages 36-44

   4. Some Insight into Intramolecular Electron Transfer of an Adrenodoxin Molecule

      • Tokuji Kimura, Taketoshi Taniguchi

      Pages 45-56

   5. Structural Studies of Electron Transfer Proteins from Sulfate Reducing Bacteria: The Amino Acid Sequence of Two Rubredoxins Isolated from Desulfovibrio Vulgaris and Desulfovibrio Gigas

      • Mireille Bruschi, Jean Le Gall

      Pages 57-67

   6. The Iron-Sulfur Centers and the Function of Hydrogenase from Clostridium Pasteurianum

      • Jiann-Shin Chen, Leonard E. Mortenson, Graham Palmer

      Pages 68-82

   7. Sequence Investigation of the Clostridium Pasteurianum Nitrogenase: the Partial Amino Acid Sequence of Azoferredoxin

      • Masaru Tanaka, Mitsuru Haniu, Kerry T. Yasunobu, Leonard E. Mortenson

      Pages 83-90

   8. On the Nature of an Intermediate that is Formed during the Enzymatic Conversion of Phenylalanine to Tyrosine

      • Seymour Kaufman

      Pages 91-102

   9. Some Properties of Bovine Pineal Tryptophan Hydroxylase

      • Arata Ichiyama, Hiroyuki Hasegawa, Chiharu Tohyama, Chieko Dohmoto, Tohru Kataoka

      Pages 103-117

   10. Evidence for Participation of NADH-Dependent Reductase in the Reaction of Benzoate 1,2-Dioxygenase (Benzoate Hydroxylase)

       • Hitoshi Fujisawa, Mutsuo Yamaguchi, Takashi Yamauchi

       Pages 118-126

   11. Subunit Structure of Nonheme Iron-Containing Dioxygenases

       • Mitsuhiro Nozaki, Ryotaro Yoshida, Chieko Nakai, Masayoshi Iwaki, Yukikazu Saeki, Hiroyuki Kagamiyama

       Pages 127-136

3. Iron-Sulfur Proteins and Heme Proteins of the Mitochondrial Electron Transport System

   1. Iron-Sulfur Proteins, the Most Numerous and Most Diversified Components of the Mitochondrial Electron Transfer System

      • Helmut Beinert

      Pages 137-149

   2. Composition and Enzymatic Properties of the Mitochondrial NADH- and NADPH-Ubiquinone Reductase (Complex I)

      • Youssef Hatefi

      Pages 150-160

   3. Factors Controlling the Turnover Number of Succinate Dehydrogenase: A New Look at an Old Problem

      • B. A. C. Ackrell, E. B. Kearney, P. Mowery, T. P. Singer, H. Beinert, A. D. Vinogradov et al.

      Pages 161-181

   4. Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase

      • Tsoo E. King, Tomoko Ohnishi, Daryl B. Winter, J. T. Wu

      Pages 182-227

   5. Heme a and Copper Environments in Cytochrome Oxidase

      • Yutaka Orii, Satoshi Yoshida, Tetsutaro Iizuka

      Pages 228-239

   6. Heme Interactions in Pseudomonas Cytochrome Oxidase

      • David C. Wharton, Kristina Hill, Quentin H. Gibson

      Pages 240-253

4. Other Heme and Non-Heme Fe-Proteins

   1. Equilibrium States and Dynamic Reactions of Iron in the Camphor Monoxygenase System

      • I. C. Gunsalus, S. G. Sligar

      Pages 254-262

   2. Current Status of the Sequence Studies of the Pseudomonas Putida Camphor Hydroxylase System

      • Masaru Tanaka, Scott Zeitlin, Kerry T. Yasunobu, I. C. Gunsalus

      Pages 263-269

An Fe- and Cu-Protein Symposium was held on December 15-18, 1975 at the East West Center-University of Hawaii and was sponsored by the United States-Japan Cooperative Science Program under the auspices of the National Science Foundation and the Japan Society for the Promotion of Science. It was recognized by the organizers of the symposium that metalloproteins are very important in the field of health science and a subject worthy of discussion by experts from the United States, Japan and Europe. The meeting was restricted to Fe- and Cu-proteins but this is still a very broad subject matter and therefore, selected topics of current interest in this field were chosen. This book contains the collected papers from most of the symposium participants. The subject matter covered in this book is divided into four parts. These are: 1) the iron-sulfur proteins (which are not a part of the mitochondrial electron transport system); 2) the iron-sulfur proteins and heme proteins of the mitochondrial electron transport system; 3) other heme and nonheme iron proteins; and 5) selected copper proteins. The organizers of the symposium wish to express their gratitude to the participants, the session chairmen, and Drs. I.C. Gunsalus and E. Frieden who assisted in the organization of the symposium.

• Alanin
• Chloroplast
• Oxidation
• amino acid
• base
• biology
• catalysis
• chemistry
• enzyme
• enzymes
• iron
• mitochondria
• protein
• proteins
• synthesis

• University of Hawaii School of Medicine, Honolulu, USA

  Kerry T. Yasunodu, Howard F. Mower

• Kyoto University Faculty of Medicine, Kyoto, Japan

  Osamu Hayaishi

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