The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping.
Biochem J
; 475(7): 1353-1370, 2018 04 16.
Article
em En
| MEDLINE
| ID: mdl-29555844
ABSTRACT
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 (H2) 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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Base de dados:
MEDLINE
Assunto principal:
Bombas de Próton
/
Escherichia coli
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Hidrogênio
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Hidrogenase
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article