Reversible hydrogenase of Anabaena variabilis ATCC 29413: catalytic properties and characterization of redox centres

FEBS Letters

Serebryakova, Larissa T.¹  Medina, Milagros²  Zorin, Nikolay A.¹  Cammack, Richard²  Gogotov, Ivan N.¹ 

[1] Institute of Soil Science and Photosynthesis, Russian Academy of Sciences, Pushchino, 142292 Moscow Region, Russia;Centre for the Study of Metals in Biology and Medicine, Division of Life Sciences, King's College, Campden Hill Rd, London W8 7AH, UK

关键词: Hydrogenase;    EPR spectroscopy;    Iron-sulfur protein;    Nickel;    Flavoprotein;    Cyanobacterium;    A.;    Anabaena;    Al.;    Alcaligenes;    An.;    Anacystis;    BV;    benzyl viologen;    EPR;    electron paramagnetic resonance spectroscopy;    Mes;    2-(N-morpholino)ethanesulphonate;    MV;    methyl viologen;   

DOI  :  10.1016/0014-5793(96)00228-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 μM), 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.

【 授权许可】

Unknown