The proceedings of the NATO Advanced Research Workshop on Biological Electron Transfer Chains contains reports on three themes. (a) Electron transfer: The analysis of ET at the molecular level is still fundamental to an understanding of how ET chains operate in vivo. After 40 years of research, the contours of the subject are now becoming clear. (b) Bacterial redox chains: These contributions show how complicated these chains can be, often involving a number of gene clusters, each of which in turn consists of an extensive array of genes. Our understanding of the regulatory aspects of these chains is only just beginning to emerge. (c) Structure and function of redox proteins: Structural information on proteins remains indispensable to a proper understanding of their function and of the context in which they operate. The two final chapters deal with oxido-reductases and the cytochrome oxidase family.

Klappentext

The proceedings of the NATO Advanced Research Workshop on Biological Electron Transfer Chains contains reports on three themes. (a) Electron transfer: The analysis of ET at the molecular level is still fundamental to an understanding of how ET chains operate in vivo. After 40 years of research, the contours of the subject are now becoming clear. (b) Bacterial redox chains: These contributions show how complicated these chains can be, often involving a number of gene clusters, each of which in turn consists of an extensive array of genes. Our understanding of the regulatory aspects of these chains is only just beginning to emerge. (c) Structure and function of redox proteins: Structural information on proteins remains indispensable to a proper understanding of their function and of the context in which they operate. The two final chapters deal with oxido-reductases and the cytochrome oxidase family.

Inhalt

Preface. 1: Biological Electron Transfer. Respiratory Electron Transfer Chains; P.L. Dutton, et al. Protein-Mediated Electron Transfer: Pathways, Orbital Interactions, and Contact-Maps. Structure-Function Relations for Protein Electron Transfer; D.N. Beratan, S.S. Skourtis. Coupling of Electron Transfer and Protein Dynamics; A.I. Kotelnikov, et al. Recent Surprises in the Study of Photoinduced Electron Transfer: Covalent versus Non-Covalent Pathways; J.W. Verhoeven, et al. Mechanisms and Control of Electron Transfer Processes in Proteins; O. Farver, I. Pecht. 2: Redox Chains: Composition and Control. The Paracoccus denitrificans Electron Transport System: Aspects of Organisation, Structures and Biogenesis; S.J. Ferguson. Genetics and Regulation of C1 Metabolism in Methylotrophs; M.E. Lidstrom, et al. Hierarchical Control of Electron-Transfer; H.V. Westerhoff, et al. On the Mechanism of Nitrite Reductase: Complex between Pseudoazurin and Nitrite Reductase from A. Cycloclastes; M.E.P. Murphy, et al. Structural Research on the Methylamine Dehydrogenase Redox Chain of Paracoccus denitrificans; F.S. Matthews, et al. 3: Oxido-Reductases: Structure and Function. Microbial Amine Oxidoreductases. Their Diversity, Role, Structure and Mechanism; J.A. Duine, A. Hacisalihoglu. Flavocytochromes: Nature's Electrical Transformers; S.K. Chapman, et al. The Chemistry of Biological Denitrification. Spectroscopic Studies Provide Insights into the Mechanism of Dissimilatory Heme cd1 and Copper-Containing Nitride Reductases; B.A. Averill, et al. Cytochrome c Nitrite Reductase from Sulfospirillum deleyianum and Wolinella succinogenes. Molecular and Spectroscopic Properties of the Multihaem Enzyme; O. Einsle, et al. Molecular Basis for Energy Transduction: Mechanisms of Cooperativity in Multihaem Cytochromes; R.O. Louro, et al. The Solution Structure of Redox Proteins and Beyond; L. Bianci, et al. 4: The Cytochrome c Oxidase Family. Exploring the Proton Channels of Cytochrome Oxidase; R.B. Gennis. Control of Electron Transfer to the Binuclear Center in Cu-Heme Oxidases; M. Brunori, et al. Chimeric Quinol Oxidases Expressed in Paracoccus denitrificans; C. Winterstein, et al. Superfamily of Cytochrome Oxidases; M. Saraste, et al. The Electron Transfer Centers of Nitric Oxide Reductase: Homology with the Heme-Copper Oxidase Family; A. Kannt, et al.