期刊
BIOCHEMICAL JOURNAL
卷 475, 期 -, 页码 1353-1370出版社
PORTLAND PRESS LTD
DOI: 10.1042/BCJ20180053
关键词
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资金
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/N006321/1]
- BBSRC EASTBIO Doctoral Training Partnership award [1510231, 1280664]
- Dakota Foundation
- Royal Society
- BBSRC [BB/L009722/1, BB/I022309/1, BB/N006321/1, BB/I02008X/1] Funding Source: UKRI
- EPSRC [EP/J013501/1] Funding Source: UKRI
Under anaerobic conditions, Escherichia coli is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from hydrogen (H-2) oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightly bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein (HybB). To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of Hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In the present paper, we describe a new overexpression system that has facilitated the determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex.
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