期刊
NATURE CHEMICAL BIOLOGY
卷 13, 期 5, 页码 544-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.2335
关键词
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资金
- Fundacao para a Ciencia e Tecnologia (FCT/MCTES) [PTDC/BBB-BEP/0934/2012, PTDC/BBB-BEP/2885/2014]
- FCT/MCTES [UID/Multi/04551/2013, LISBOA-01-0145-FEDER-007660]
- FEDER funds through COMPETE2020-Programa Operacional Competitividade e Internacionalizacao (POCI)
- Spanish MINECO/FEDER project [CTQ2015-71290-R]
- MINECO [BES-2013-064099]
- European Community [283570]
- [SFRH/BD/60879/2009]
- Fundação para a Ciência e a Tecnologia [PTDC/BBB-BEP/0934/2012, SFRH/BD/60879/2009] Funding Source: FCT
Hydrogenases are highly active enzymes for hydrogen production and oxidation. [NiFeSe] hydrogenases, in which selenocysteine is a ligand to the active site Ni, have high catalytic activity and a bias for H-2 production. In contrast to [NiFe] hydrogenases, they display reduced H-2 inhibition and are rapidly reactivated after contact with oxygen. Here we report an expression system for production of recombinant [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough and study of a seleno-cysteine-to-cysteine variant (Sec489Cys) in which, for the first time, a [NiFeSe] hydrogenase was converted to a [NiFe] type. This modification led to severely reduced Ni incorporation, revealing the direct involvement of this residue in the maturation process. The Ni-depleted protein could be partly reconstituted to generate an enzyme showing much lower activity and inactive states characteristic of [NiFe] hydrogenases. The Ni-Sec489Cys variant shows that selenium has a crucial role in protection against oxidative damage and the high catalytic activities of the [NiFeSe] hydrogenases.
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