Molybdenum enzymes, cofactors, and model systems : developed from a symposium sponsored by the Division of Inorganic Chemistry at the 204th National Meeting of the American Chemical Society, Washington, DC, August 23-28, 1992
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Bibliographic Information
Molybdenum enzymes, cofactors, and model systems : developed from a symposium sponsored by the Division of Inorganic Chemistry at the 204th National Meeting of the American Chemical Society, Washington, DC, August 23-28, 1992
（ACS symposium series, 535）
American Chemical Society, 1993
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Includes bibliographical references and index
Description and Table of Contents
Description
Focusing on recent advances in the molybdenum enzymes Moco and FeMoco and their model systems, this study: discusses the recent crystallographic determination of the structure of the molybdenum-iron protein in the nitrogenase enzyme; highlights the latest results on the molybdenum cofactor Moco, including the full organic structure that has just been determined; and includes an overview of molybdenum in biology and the role of molybdoenzymes in the nitrogen, sulfer and carbon cycles.
Table of Contents
- Molybdenum enzymes, cofactors and chemistry - an introductory survey, Edward I. Stiefel. Part 1 Molybdenum cofactor enzymes: the reaction mechanism of xanthine oxidase, Russ Hille
- biochemistry of the molybdenum cofactors, K.V. Rajagopalan
- the bacterial Oxmolybdenum cofactor, O. Meyer et al. Part 2 Molybdenum cofactor models: models of pterin-containing molybdenum enzymes, Charles G. Young and Anthony G. Wedd
- pterins, quinoxalines and metallo-ene-dithiolates - synthetic approach to the molybdenum cofactor, Robert S. Pilato et al
- strategies for the synthesis of the cofactor of the oxomolybdoenzymes, C.D. Garner et al
- molybdenum complexes of reduced pterins, Sharon J. Nieter Burgmayer et al
- chemical and physical coupling of oxomolybdenum centres and iron porphyrins - models for the molybdenum-iron interaction in sulfite oxidase, Michael J. LaBarre et al. Part 3 Nitrogenase: nitrogenase structure, function and genetics, Barbara K. Burgess
- crystal structures of the iron protein and molybdenum-iron protein of nitrogenase, D.C. Rees et al
- structure and environment of metal clusters in the nitrogenase molybdenum-iron protein from clostridium pasteurianum, Jeffrey T. Bolin et al
- biosynthesis of the iron-molybdenum cofactor of nitrogenase, Paul W. Ludden et al
- role of the iron-molybdenum cofactor polypeptide environment in azotobacter vinelandii molybdenum-nitrogenase catalysis
- extended x-ray absorption fine structure and L-Edge spectroscopy of nitrogenase molybdenum-iron protein J. Chen et al
- redox properties of the nitrogenase proteins from azotobader vinelandii, G.D. Watt et al
- the molybdenum-iron protein of nitrogenase - structural and functional features of metal cluster prosthetic groups, W.H. Orme-Johnson
- protein component complex formation and adenosine triphosphate hydrolysis in nitrogenase, James Bryant Howard
- electron-transfer reactions associated with nitrogenase from klebsiellia pneumoniae R.N.F. Thorneley et al
- Part 4 Nitrogenase models: recent structure determinations of the molybdenum-iron protein of nitrogenase - impact on design of synthetic analogs for the iron-molybednum-sulfur analogs for the iron-molybdenum-sulfur active site and the iron-molybdenum cofactor, Dimitri Coucouvanis. Part of contents.
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