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Reversible hydrogenase of Anabaena variabilis ATCC 29413: catalytic properties and characterization of redox centres
Author(s) -
Serebryakova Larissa T.,
Medina Milagros,
Zorin Nikolay A.,
Gogotov Ivan N.,
Cammack Richard
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00228-1
Subject(s) - hydrogenase , anabaena variabilis , chemistry , photochemistry , electron paramagnetic resonance , catalysis , redox , nickel , flavin group , carbon monoxide , enzyme , inorganic chemistry , biochemistry , cyanobacteria , biology , nuclear magnetic resonance , organic chemistry , bacteria , physics , genetics
The catalytic and spectroscopic properties of the reversible hydrogenase from the cyanobacterium Anabaena variabilis have been examined. The hydrogenase required reductive activation in order to elicit hydrogen‐oxidation activity. Carbon monoxide was a weak ( K i = 35 μ M), reversible and competitive inhibitor. A flavin with the chromatographic properties of FMN, and nickel were detected in the purified enzyme. A. variabilis hydrogenase exhibited electron paramagnetic resonance (EPR) spectra in its hydrogen‐reduced state, indicative of [2Fe‐2S] and [4Fe‐4S] clusters. Although no EPR signals due to nickel were detected, the results are consistent with the enzyme being a flavin‐containing hydrogenase of the nickel‐iron type.