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

FEBS Letters
L T SerebryakovaR Cammack

Abstract

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 (Ki=35 microM), 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.

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Citations

May 30, 2002·Biochimica Et Biophysica Acta·Oliver SchmitzThomas Happe
Mar 5, 2002·Microbiology and Molecular Biology Reviews : MMBR·Paula TamagniniPeter Lindblad
Sep 14, 2006·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Minnan LongSimon P J Albracht
Jun 17, 2011·Journal of the American Chemical Society·Chelsea L McIntoshAnne K Jones
Mar 23, 2017·Genetics and Molecular Biology·Alberto A Esteves-FerreiraWagner L Araújo
Jan 14, 2017·Frontiers in Genetics·Vincenzo PuggioniAmel Latifi
Jun 15, 2006·Briefings in Functional Genomics & Proteomics·Martin E Barrios-LlerenaPhillip C Wright
Dec 29, 2020·Chemical Communications : Chem Comm·David W MulderSimone Raugei
May 1, 1997·Applied and Environmental Microbiology·P TamagniniP Lindblad

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