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PDBsum entry 5oef
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Oxidoreductase
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PDB id
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5oef
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References listed in PDB file
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Key reference
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Title
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Chalcogenide substitution in the [2fe] cluster of [fefe]-Hydrogenases conserves high enzymatic activity.
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Authors
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L.Kertess,
F.Wittkamp,
C.Sommer,
J.Esselborn,
O.Rüdiger,
E.J.Reijerse,
E.Hofmann,
W.Lubitz,
M.Winkler,
T.Happe,
U.P.Apfel.
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Ref.
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Dalton Trans, 2017,
46,
16947-16958.
[DOI no: ]
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PubMed id
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Abstract
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[FeFe]-Hydrogenases efficiently catalyze the uptake and evolution of
H2due to the presence of an inorganic [6Fe-6S]-cofactor (H-cluster).
This cofactor is comprised of a [4Fe-4S] cluster coupled to a unique [2Fe]
cluster where the catalytic turnover of H2/H+takes place.
We herein report on the synthesis of a selenium substituted [2Fe] cluster
[Fe2{μ(SeCH2)2NH}(CO)4(CN)2]2-(ADSe)
and its successful in vitro integration into the native protein scaffold of
[FeFe]-hydrogenases HydA1 from Chlamydomonas reinhardtii and CpI from
Clostridium pasteurianum yielding fully active enzymes (HydA1-ADSe and
CpI-ADSe). FT-IR spectroscopy and X-ray structure analysis confirmed the
presence of structurally intact ADSe at the active site. Electrochemical assays
reveal that the selenium containing enzymes are more biased towards hydrogen
production than their native counterparts. In contrast to previous chalcogenide
exchange studies, the S to Se exchange herein is not based on a simple
reconstitution approach using ionic cluster constituents but on the in vitro
maturation with a pre-synthesized selenium-containing [2Fe] mimic. The
combination of biological and chemical methods allowed for the creation of a
novel [FeFe]-hydrogenase with a [2Fe2Se]-active site which confers individual
catalytic features.
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