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一种关于血红素-铜氧化酶中质子泵浦机制的化学显式模型。

A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases.

作者信息

Sharpe Martyn A, Ferguson-Miller Shelagh

机构信息

Department of Neurosurgery, The Methodist Hospital, Houston, TX 77030, USA.

出版信息

J Bioenerg Biomembr. 2008 Oct;40(5):541-9. doi: 10.1007/s10863-008-9182-6. Epub 2008 Oct 1.

DOI:10.1007/s10863-008-9182-6
PMID:18830692
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2613019/
Abstract

A mechanism for proton pumping is described that is based on chemiosmotic principles and the detailed molecular structures now available for cytochrome oxidases. The importance of conserved water positions and a step-wise gated process of proton translocation is emphasized, where discrete electron transfer events are coupled to proton uptake and expulsion. The trajectory of each pumped proton is the same for all four substrate electrons. An essential role for the His-Tyr cross-linked species is discussed, in gating of the D- and K-channels and as an acceptor/donor of electrons and protons at the binuclear center.

摘要

描述了一种基于化学渗透原理和目前已有的细胞色素氧化酶详细分子结构的质子泵浦机制。强调了保守水位置和质子转运的逐步门控过程的重要性,其中离散的电子转移事件与质子的摄取和排出相耦合。对于所有四个底物电子,每个泵浦质子的轨迹都是相同的。讨论了His-Tyr交联物种在D通道和K通道的门控以及作为双核中心电子和质子的受体/供体方面的重要作用。

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本文引用的文献

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EPR evidence of cyanide binding to the Mn(Mg) center of cytochrome c oxidase: support for Cu(A)-Mg involvement in proton pumping.电子顺磁共振证明氰化物与细胞色素c氧化酶的锰(镁)中心结合:支持铜(A)-镁参与质子泵浦
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Electrostatic basis for the unidirectionality of the primary proton transfer in cytochrome c oxidase.细胞色素c氧化酶中初级质子转移单向性的静电基础。
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Heme-heme communication during the alkaline-induced structural transition in cytochrome c oxidase.细胞色素c氧化酶碱性诱导结构转变过程中的血红素-血红素通讯
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Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant.E286H突变体的主链酰胺氢-氘交换揭示的细胞色素c氧化酶质子转运所涉及的结构元件
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