Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation

From May 3-7,1997, the NATO Advanced Research Workshop on 'Biological Electron Transfer Chains' was organized in Tomar, Portugal. In the application for support the choice of the topic was justified as follows: "[Until recently efforts] have concentrated on the study of the structure and function of individual redox enzymes and proteins. Enough information is now available to make a start with the study of biological electron transfer (E1) at the next higher level of organization, that of the complete ET chain." The interest in the workshop was high: the majority of participants had registered before the workshop was formally announced, which illustrates the popularity of the topic within the biochemical and biophysical communities. The present volume contains a number of reports based on the lectures presented by the key speakers during the meeting. The workshop dealt with the following three themes: a) Electron transfer, which is the subject of Chapter 1. The analysis of ET at the molecular level is still fundamental for an understanding of how ET chains operate in vivo. After 40 years of research the contours of the subject are becoming clear now. b) Bacterial redox chains. This is the subject of Chapter 2. Its contents show how complicated these chains can be, often involving a number of gene clusters. Our understanding of the regulatory aspects and control mechanisms of these chains is only in its beginning.

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 MultihaemEnzyme; 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.