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Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H-2 supports its catalytic relevance

Senger, Moritz (author)
Uppsala universitet,Fysikalisk kemi
Kernmayr, Tobias (author)
Ludwig Maximilians Univ Munchen, Dept Chem, D-81377 Munich, Germany.
Lorenzi, Marco (author)
Uppsala universitet,Molekylär biomimetik
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Redman, Holly J. (author)
Berggren, Gustav (author)
Uppsala universitet,Molekylär biomimetik
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 (creator_code:org_t)
2022
2022
English.
In: Chemical Communications. - : Royal Society of Chemistry (RSC). - 1359-7345 .- 1364-548X. ; 58:51, s. 7184-7187
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Small molecules in solution may interfere with mechanistic investigations, as they can affect the stability of catalytic states and produce off-cycle states that can be mistaken for catalytically relevant species. Here we show that the hydride state (H-hyd), a proposed central intermediate in the catalytic cycle of [FeFe]-hydrogenase, can be formed in wild-type [FeFe]-hydrogenases treated with H-2 in absence of other, non-biological, reductants. Moreover, we reveal a new state with unclear role in catalysis induced by common low pH buffers.

Subject headings

NATURVETENSKAP  -- Kemi -- Organisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Organic Chemistry (hsv//eng)

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