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Titlebook: Metallocofactors that Activate Small Molecules; With Focus on Bioino Markus W. Ribbe Book 2019 Springer Nature Switzerland AG 2019 Nitrogen

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发表于 2025-3-21 18:37:49 | 显示全部楼层 |阅读模式
书目名称Metallocofactors that Activate Small Molecules
副标题With Focus on Bioino
编辑Markus W. Ribbe
视频video
概述Presents an overview of the fundamental chemistry of metallocofactors within the field of bioinorganic chemistry.Provides a review of the mechanistic understanding of metallocofactors.Multi-authored v
丛书名称Structure and Bonding
图书封面Titlebook: Metallocofactors that Activate Small Molecules; With Focus on Bioino Markus W. Ribbe Book 2019 Springer Nature Switzerland AG 2019 Nitrogen
描述This volume highlights recent progress on the fundamental chemistry and mechanistic understanding of metallocofactors, with an emphasis on the major development in these areas from the perspective of bioinorganic chemistry. .Metallocofactors are essential for all forms of life and include a variety of metals, such as iron, molybdenum, vanadium, and nickel. Structurally fascinating metallocofactors featuring these metals are present in many bacteria and mediate remarkable metabolic redox chemistry with small molecule substrates, including N2, CO, H2, and CO2. Current interest in understanding how these metallocofactors function at the atomic level is enormous, especially in the context of sustainably feeding and fueling our planet; if we can understand how these cofactors work, then there is the possibility to design synthetic catalysts that function similarly. .
出版日期Book 2019
关键词Nitrogenase; Molybdopterin; Molybdopterin Models; Carbon Monoxide Dehydrogenase; Nitrogenase Cofactors; P
版次1
doihttps://doi.org/10.1007/978-3-030-25897-9
isbn_softcover978-3-030-25899-3
isbn_ebook978-3-030-25897-9Series ISSN 0081-5993 Series E-ISSN 1616-8550
issn_series 0081-5993
copyrightSpringer Nature Switzerland AG 2019
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https://doi.org/10.1007/978-3-030-25897-9Nitrogenase; Molybdopterin; Molybdopterin Models; Carbon Monoxide Dehydrogenase; Nitrogenase Cofactors; P
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Structure and Bondinghttp://image.papertrans.cn/m/image/631570.jpg
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Looking at Nitrogenase: Insights from Modern Structural Approaches,sm of nitrogen reduction to ammonia. Previously, structural studies have contributed to determining the arrangement and identity of the unique metallocofactors of the as-isolated nitrogenase enzyme. Due to the multi-protein, dynamic nature of catalysis in nitrogenase, structurally capturing intermed
发表于 2025-3-22 17:38:52 | 显示全部楼层
Current Understanding of the Biosynthesis of the Unique Nitrogenase Cofactor Core,ied Mo-nitrogenase utilizes a complex metallocofactor ([MoFe.S.C(.-homocitrate)]) for substrate binding and reduction; however, the complexity of this cofactor has hindered a better understanding of its mechanistic details and chemical synthesis so far. Driven by the pressing questions related to th
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The Catalytic Mechanisms of the Molybdenum and Tungsten Enzymes,single exception are found in association with a novel pyranopterin dithiolene cofactor called molybdopterin. This review focusses on the catalytic mechanisms of the molybdenum and tungsten enzymes, with an emphasis on the molybdenum and tungsten sites. Most, but not all, of the enzymes catalyze oxy
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