Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation
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- 作者：Motoaki Sato (1) (2)
Jesus Torres-Bacete (1) (3)
Prem Kumar Sinha (1) (4)
Akemi Matsuno-Yagi (1)
Takao Yagi (1) - 关键词：NADH Dehydrogenase ; Complex I ; NDH ; 1 ; Genetic engineering ; Proton translocation ; Escherichia coli
- 刊名：Journal of Bioenergetics and Biomembranes
- 出版年：2014
- 出版时间：August 2014
- 年：2014
- 卷：46
- 期：4
- 页码：279-287
- 全文大小：1,445 KB
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Jesus Torres-Bacete (1) (3)
Prem Kumar Sinha (1) (4)
Akemi Matsuno-Yagi (1)
Takao Yagi (1)
1. Department of Molecular and Experimental Medicine, MEM-256, The Scripps Research Institute, La Jolla, CA, 92037, USA
2. Department of Biological Research, Odawara Research Center, Nippon Soda Co., Ltd., Odawara, 250-0280, Japan
3. Centro de investigaciones Biologicas del CSIC, Madrid, 28040, Spain
4. College of Medicine, Pennsylvania State University, Hershey, PA, USA - ISSN：1573-6881
文摘
The proton-translocating NADH-quinone oxidoreductase (complex I/NDH-1) is the first and largest enzyme of the respiratory chain which has a central role in cellular energy production and is implicated in many human neurodegenerative diseases and aging. It is believed that the peripheral domain of complex I/NDH-1 transfers the electron from NADH to Quinone (Q) and the redox energy couples the proton translocation in the membrane domain. To investigate the mechanism of the proton translocation, in a series of works we have systematically studied all membrane subunits in the Escherichia coli NDH-1 by site-directed mutagenesis. In this mini-review, we have summarized our strategy and results of the mutagenesis by depicting residues essential for proton translocation, along with those for subunit connection. It is suggested that clues to understanding the driving forces of proton translocation lie in the similarities and differences of the membrane subunits, highlighting the communication of essential charged residues among the subunits. A possible proton translocation mechanism with all membrane subunits operating in unison is described.