The Alternative complex III: Properties and possible mechanisms for electron transfer and energy conservation

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• 作者：Patr¨ªcia N. Refojo ; Miguel Teixeira ; Manuela M. Pereira
• 关键词：ACIII ; alternative complex III ; HiPIP ; high-potential iron&ndash ; sulfur protein ; R ; Rhodothermus ; C ; Chloroflexus ; CISM ; complex iron&ndash ; sulfur molybdoenzyme ; MGD ; molybdopterin-guanine dinucleotide ; TMAO ; trimethylamine N-oxide ; DMSO ; dimethyl sulfoxi
• 刊名：Biochimica et Biophysica Acta (BBA)/Bioenergetics
• 出版年：2012
• 出版时间：October, 2012
• 年：2012
• 卷：1817
• 期：10
• 页码：1852-1859
• 全文大小：653 K

文摘

Alternative complexes III (ACIII) are recently identified membrane-bound enzymes that replace functionally the cytochrome bc_1/b₆f complexes. In general, ACIII are composed of four transmembrane proteins and three peripheral subunits that contain iron-sulfur centers and C-type hemes. ACIII are built by a combination of modules present in different enzyme families, namely the complex iron-sulfur molybdenum containing enzymes. In this article a historical perspective on the investigation of ACIII is presented, followed by an overview of the present knowledge on these enzymes. Electron transfer pathways within the protein are discussed taking into account possible different locations (cytoplasmatic or periplasmatic) of the iron-sulfur containing protein and their contribution to energy conservation. In this way several hypotheses for energy conservation modes are raised including linear and bifurcating electron transfer pathways. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).