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O 2 Inhibition of Ni‐Containing CO Dehydrogenase Is Partly Reversible
Author(s) -
Merrouch Meriem,
HadjSaïd Jessica,
Domnik Lilith,
Dobbek Holger,
Léger Christophe,
Dementin Sébastien,
Fourmond Vincent
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201502835
Subject(s) - desulfovibrio vulgaris , reactivity (psychology) , chemistry , carbon monoxide dehydrogenase , cyclic voltammetry , catalysis , combinatorial chemistry , stereochemistry , bacteria , electrochemistry , biochemistry , electrode , carbon monoxide , biology , genetics , alternative medicine , medicine , pathology
Ni‐containing CO dehydrogenases (CODHs) are very efficient metalloenzymes that catalyze the conversion between CO 2 and CO. They are a source of inspiration for designing CO 2 ‐reduction catalysts and can also find direct use in biotechnology. They are deemed extremely sensitive to O 2 , but very little is known about this aspect of their reactivity. We investigated the reaction with O 2 of Carboxydothermus hydrogenoformans ( Ch ) CODH II and the homologous, recently characterized CODH from Desulfovibrio vulgaris ( Dv ) through protein film voltammetry and solution assays (in the oxidative direction). We found that O 2 reacts very quickly with the active site of CODHs, generating species that reactivate upon reduction—this was unexpected. We observed that distinct CODHs exhibit different behaviors: Dv CODH reacts half as fast with O 2 than Ch CODH, and only the former fully recovers the activity upon reduction. The results raise hope that fast CO/CO 2 biological conversion may be feasible under aerobic conditions.