Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

doi:10.1016/j.febslet.2006.09.062

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	Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus
	Peng, Guohong ; Bostina, Mihnea ; Radermacher, Michael ; Rais, Isam ; Karas, Michael ; Michel, Hartmut
刊名	FEBS LETTERS
	2006-10-30
卷号	580 期号:25 页码:5934-5940
关键词	F1f0 Atpase b Subunit Mass Spectrometric Identification Electron Microscopic Single Particle Analysis Aquifex Aeolicus
ISSN号	0014-5793
DOI	10.1016/j.febslet.2006.09.062
文献子类	Article
英文摘要	The F1F0 ATP synthase has been purified from the hyperthermophilic eubacterium Aquifex aeolicus and characterized. Its subunits have been identified by MALDI-mass spectrometry through peptide mass fingerprinting and MS/MS. It contains the canonical subunits alpha, beta, gamma, delta and epsilon of F-1 and subunits a and c of F-0. Two versions of the b subunit were found, which show a low sequence homology to each other. Most likely they form a heterodimer. An electron microscopic single particle analysis revealed clear structural details, including two stalks connecting F-1 and F-0. In several orientations the central stalk appears to be tilted and/or kinked. It is unclear whether there is a direct connection between the peripheral stalk and the 6 subunit. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.; The F1F0 ATP synthase has been purified from the hyperthermophilic eubacterium Aquifex aeolicus and characterized. Its subunits have been identified by MALDI-mass spectrometry through peptide mass fingerprinting and MS/MS. It contains the canonical subunits alpha, beta, gamma, delta and epsilon of F-1 and subunits a and c of F-0. Two versions of the b subunit were found, which show a low sequence homology to each other. Most likely they form a heterodimer. An electron microscopic single particle analysis revealed clear structural details, including two stalks connecting F-1 and F-0. In several orientations the central stalk appears to be tilted and/or kinked. It is unclear whether there is a direct connection between the peripheral stalk and the 6 subunit. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
学科主题	Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
URL标识	查看原文
语种	英语
WOS记录号	WOS:000241707100021
公开日期	2010-12-24
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/5899]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Max Planck Inst Biophys, D-60438 Frankfurt, Germany 2.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 3.Univ Vermont, Dept Physiol & Mol Biophys, Burlington, VT 05405 USA 4.Univ Frankfurt, Inst Pharmaceut Chem, D-60439 Frankfurt, Germany
推荐引用方式 GB/T 7714	Peng, Guohong,Bostina, Mihnea,Radermacher, Michael,et al. Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus[J]. FEBS LETTERS,2006,580(25):5934-5940.
APA	Peng, Guohong,Bostina, Mihnea,Radermacher, Michael,Rais, Isam,Karas, Michael,&Michel, Hartmut.(2006).Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus.FEBS LETTERS,580(25),5934-5940.
MLA	Peng, Guohong,et al."Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus".FEBS LETTERS 580.25(2006):5934-5940.