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Titlebook: Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling; William A. Cramer,Toivo Kallas Book 2016 Springer Science

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发表于 2025-3-21 16:29:56 | 显示全部楼层 |阅读模式
书目名称Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling
编辑William A. Cramer,Toivo Kallas
视频videohttp://file.papertrans.cn/243/242606/242606.mp4
概述Encyclopedic discussion of multi-faceted functions in energy transduction, evolution, and signaling.Perspective on a major group of integral membrane proteins.Modern review of the cytochrome family ex
丛书名称Advances in Photosynthesis and Respiration
图书封面Titlebook: Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling;  William A. Cramer,Toivo Kallas Book 2016 Springer Science
描述.An Introduction that describes the origin of cytochrome notation also connects to the history of the field, focusing on research in England in the pre-World War II era.  The start of the modern era of studies on structure-function of cytochromes and energy-transducing membrane proteins was marked by the 1988 Nobel Prize in Chemistry, given to J. Deisenhofer, H. Michel, and R. Huber for determination of the crystal structure of the bacterial photosynthetic reaction center. An .ab initio. logic of presentation in the book discusses the evolution of cytochromes and hemes, followed by theoretical perspectives on electron transfer in proteins and specifically in cytochromes. There is an extensive description of the molecular structures of cytochromes and cytochrome complexes from eukaryotic and prokaryotic sources, bacterial, plant and animal. The presentation of atomic structure information has a major role in these discussions, and makes an important contribution to the broad field of membrane protein structure-function. .
出版日期Book 2016
关键词Cytochromes; Energy transduction; Membranes; Evolution; Signaling
版次1
doihttps://doi.org/10.1007/978-94-017-7481-9
isbn_softcover978-94-024-1356-4
isbn_ebook978-94-017-7481-9Series ISSN 1572-0233 Series E-ISSN 2215-0102
issn_series 1572-0233
copyrightSpringer Science+Business Media Dordrecht 2016
The information of publication is updating

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The Diversity of Photosynthetic Cytochromesnthetic organisms rely on cytochromes to move electrons around the cell and drive the photosynthetic mechanism. Although cytochromes have many jobs in many environments, only a few types of cytochromes are involved in these electron transport chains. The hemes vary in axial ligation to meet the need
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Evolution of Photosynthetic NDH-1: Structure and Physiological Functionnase present in bacteria and mitochondria (respiratory NDH-1). They both have a common ancestor, namely the group 4 membrane-bound hydrogenases, including energy-converting hydrogenase (Ech). During its evolution, respiratory NDH-1 (complex 1) acquired the electron input N module that functions in N
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Fundamentals of Electron Transfer in Proteinsncepts rather than on mathematical details. The reorganization energy has been considered as well as the dependence of the activation energy on this parameter and on the reaction energy. The quantum—mechanical treatment of the pre-exponential factor is described, and the regularities of the non-adia
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Theoretical Analysis of Electron Transfer in Proteins: From Simple Proteins to Complex Machinerieser bioenergetic processes such as denitrification or sulfate and sulfite reduction. Moreover, electron transfer is a key step in many enzymatic reactions. The framework of Marcus theory provides the theoretical basis to describe the kinetics of these reactions. The parameters to calculate rate const
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Cytochrome ,, in Photosystem IIn, the light-induced oxidation of water. It consists of 17 membrane-spanning α-helical and three membrane-extrinsic protein subunits and binds nearly 100 cofactors. Among them is a heme protein composed of one heme . group ligated by two low molecular weight subunits with one transmembrane helix eac
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Structure-Function of the Cytochrome ,,, Lipoprotein Complexoton-coupled electron transfer reactions that link the two light-trapping photosystem reaction centers in the electron transport chain of oxygenic photosynthesis, and contains the rate-limiting step of the entire electron transport chain. The understanding of the functions of the intra-membrane cyto
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Structure-Function Studies of the Cytochrome ,, Complex of Anoxygenic Photosynthetic Purple Bacteriaally or aerobically. The photosynthetic and respiratory branches of the power system in purple bacteria are connected via the cytochrome .. complex (cyt ..), which catalyzes electron transfer from quinol to cyt . and couples this reaction to proton translocation across the photosynthetic membrane, g
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