期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1817, 期 4, 页码 489-494出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2011.11.018
关键词
Cytochrome aa(3); Conformational change; Bile salts; Lipid binding
资金
- NIGMS NIH HHS [R01 GM026916-32A1, R01 GM026916] Funding Source: Medline
As a consumer of 95% of the oxygen we breathe, cytochrome c oxidase plays a major role in the energy balance of the cell. Regulation of its oxygen reduction and proton pumping activity is therefore critical to physiological function in health and disease. The location and structure of pathways for protons that are required to support cytochrome c oxidase activity are still under debate, with respect to their requirements for key residues and fixed waters, and how they are gated to prevent (or allow) proton backflow. Recent high resolution structures of bacterial and mammalian forms reveal conserved lipid and steroid binding sites as well as redox-linked conformational changes that provide new insights into potential regulatory ligands and gating modes. Mechanistic interpretation of these findings and their significance for understanding energy regulation is discussed. This article is part of a Special Issue entitled: Respiratory Oxidases. (C) 2011 Elsevier B.V. All rights reserved.
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