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Titlebook: Catalysts for Nitrogen Fixation; Nitrogenases, Releva Barry E. Smith,Raymond L. Richards,William E. Newt Book 2004 Springer Science+Busines

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书目名称Catalysts for Nitrogen Fixation
副标题Nitrogenases, Releva
编辑Barry E. Smith,Raymond L. Richards,William E. Newt
视频videohttp://file.papertrans.cn/223/222473/222473.mp4
丛书名称Nitrogen Fixation: Origins, Applications, and Research Progress
图书封面Titlebook: Catalysts for Nitrogen Fixation; Nitrogenases, Releva Barry E. Smith,Raymond L. Richards,William E. Newt Book 2004 Springer Science+Busines
描述.Biological nitrogen fixation provides more than 50% of the total annual input of the essential element nitrogen to world agriculture. Thus, it is of immense agronomic importance and critical to food supplies, particularly in developing countries. ..This book, with chapters authored by internationally renowned experts, provides a comprehensive and detailed account of the fascinating history of the process - including the surprising discoveries of molybdenum-independent nitrogenases and superoxide-dependent nitrogenase; a review of Man‘s attempts to emulate the biological process - most successfully with the commercially dominant Haber-Bosch process; and the current state of the understanding art with respect to the enzymes - called nitrogenases - responsible for biological nitrogen fixation. ..The initial chapters use a historical approach to the biological and industrial processes, followed by an overview of assay methodologies. The next set of chapters focuses on the classical enzyme, the molybdenum nitrogenase, and details its biosynthesis, structure, composition, and mechanism of action as well as detailing both how variants of its two component proteins are constructed by reco
出版日期Book 2004
关键词DNA; Nucleotide; biochemistry; enzymes; protein; proteins; thermodynamics
版次1
doihttps://doi.org/10.1007/978-1-4020-3611-8
isbn_softcover978-90-481-6675-6
isbn_ebook978-1-4020-3611-8
copyrightSpringer Science+Business Media Dordrecht 2004
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https://doi.org/10.1007/978-3-031-10996-6oFe protein into the Fe protein (Howard and Rees, 1994). It seems likely that this complicated series of events ensures the unidirectional flow of electrons from the Fe protein to their final destination of substrates. Electrons delivered from the Fe protein appear to be initially received by an unu
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Polydactyly and Syndactyly of the Handter detail about the properties of this family of cofactors will be presented in other chapters of this volume. Additional insight into the structure and reactivity of the FeMo-cofactor is provided in previous reviews (Smith ., 1985; Burgess, 1990; Ludden ., 1993; Allen ., 1994).
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Structural Models for the FeMo-Cofactor and the P Clusters, nitrogenase, the reduction of dinitrogen occurs at the iron-molybdenum-cofactor (FeMo-cofactor). In addition, within the protein are unusual iron-sulfur clusters, which are probably involved in electron transfer, called the P cluster. The structures of both the FeMo-cofactor and the P cluster were
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