O2 Inhibition of Ni-Containing CO Dehydrogenase Is Partly Reversible

被引:35
作者
Merrouch, Meriem [1 ]
Hadj-Said, Jessica [1 ]
Domnik, Lilith [2 ]
Dobbek, Holger [2 ]
Leger, Christophe [1 ]
Dementin, Sebastien [1 ]
Fourmond, Vincent [1 ]
机构
[1] Aix Marseille Univ, CNRS, BIP UMR 7281, F-13402 Marseille 20, France
[2] Humboldt Univ, Inst Biol Strukturbiol Biochem, D-10099 Berlin, Germany
关键词
bioinorganic chemistry; CO dehydrogenase; metalloenzymes; protein film voltammetry; CARBON-MONOXIDE DEHYDROGENASE; CARBOXYDOTHERMUS-HYDROGENOFORMANS; RHODOSPIRILLUM-RUBRUM; CLOSTRIDIUM-THERMOACETICUM; BUTYL ISOCYANIDE; NICKEL; ELECTROCHEMISTRY; INACTIVATION; ACTIVATION; CATALYSIS;
D O I
10.1002/chem.201502835
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Ni-containing CO dehydrogenases (CODHs) are very efficient metalloenzymes that catalyze the conversion between CO2 and CO. They are a source of inspiration for designing CO2-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/CO2 biological conversion may be feasible under aerobic conditions.
引用
收藏
页码:18934 / 18938
页数:5
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