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.

Klappentext

The proceedings of the NATO Advanced Research Workshop on emBiological/em emElectron Transfer Chains/em contains reports on three themes. (a) emElectron transfer/em: The analysis of ET at the molecular level is still fundamental to an understanding of how ET chains operate emin vivo/em. After 40 years of research, the contours of the subject are now becoming clear. (b) emBacterial redox chains/em: 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) emStructure and function of redox/em emproteins/em: 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
Respiratory Electron Transfer Chains.- Protein-Mediated Electron Transfer: Pathways, Orbital Interactions, and Contact-Maps. Structure-Function Relations for Protein Electron Transfer.- Coupling of Electron Transfer and Protein Dynamics.- Recent Surprises in the Study of Photoinduced Electron Transfer: Covalent versus Non-Covalent Pathways.- Mechanisms and Control of Electron Transfer Processes in Proteins.- The Paracoccus Denitrificans Electron Transport System: Aspects of Organisation, Structures and Biogenesis.- Genetics and Regulation of C1 Metabolism in Methylotrophs.- Hierarchical Control of Electron-Transfer.- On the Mechanism of Nitrite Reductase: Complex between Pseudoazurin and Nitrite Reductase from A. Cycloclastes.- Structural Research on the Methylamine Dehydrogenase Redox Chain of Paracoccus Denitrificans.- Microbial Amine Oxidoreductases. Their Diversity, Role, Structure and Mechanism.- Flavocytochromes: Nature's Electrical Transformers.- The Chemistry of Biological Denitrification. Spectroscopic Studies Provide Insights into the Mechanism of Dissimilatory Herne cd1 and Copper-Containing Nitride Reductases.- Cytochrome c Nitrite Reductase from Sulforospirillum Deleyianum and Wolinella Succinogenes. Molecular and Spectroscopic Properties of the Multihaem Enzyme.- Molecular Basis for Energy Transduction: Mechanisms of Cooperativity in Multihaem Cytochromes.- The Solution Structure of Redox Proteins and Beyond.- Exploring the Proton Channels of Cytochrome Oxidase.- Control of Electron Transfer to the Binuclear Center in Cu-Heme Oxidases.- Chimeric Quinol Oxidases Expressed in Paracoccus Denitrificans.- Superfamily of Cytochrome Oxidases.- The Electron Transfer Centers of Nitric Oxide Reductase: Homology with the Heme-Copper Oxidase Family.