Abstract
Flavocytochrome c sulfide dehydrogenase (FCC) is one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria. FCC catalyzes oxidation of sulfide and polysulfide ions to elemental sulfur accompanied by electron transfer to cytochrome c. The catalytically active form of the enzyme is a non-covalently linked heterodimer composed of flavin- and heme-binding subunits. The Thioalkalivibrio paradoxus ARh1 genome contains five copies of genes encoding homologous FCCs with an amino acid sequence identity from 36 to 54%. When growing on thiocyanate or thiosulfate as the main energy source, the bacterium synthesizes products of different copies of FCC genes. In this work, we isolated and characterized FCC synthesized during the growth of Tv. paradoxus on thiocyanate. FCC was shown to oxidize exclusively sulfide but not other reduced sulfur compounds, such as thiosulfate, sulfite, tetrathionate, and sulfur, and it also does not catalyze the reverse reaction of sulfur reduction to sulfide. Kinetic parameters of the sulfide oxidation reaction are characterized.
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Abbreviations
- CytC :
-
cytochrome c from horse heart
- FCC:
-
flavocytochrome c sulfide dehydrogenase
- TcDH:
-
thiocyanate dehydrogenase
- TpFCC:
-
flavocytochrome c sulfide dehydrogenase from the bacterium Thioalkalivibrio paradoxus ARh 1
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Funding
This study was financially supported by the Russian Science Foundation (project no. 20-14-00314; characterization of the enzyme, enzyme kinetics) and by the Ministry of Science and Higher Education of the Russian Federation (isolation of the enzyme).
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The authors declare no conflict of interest in financial or any other sphere. This article does not contain any studies with human participants or animals performed by any of the authors.
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Tikhonova, T.V., Lilina, A.V., Osipov, E.M. et al. Catalytic Properties of Flavocytochrome c Sulfide Dehydrogenase from Haloalkaliphilic Bacterium Thioalkalivibrio paradoxus. Biochemistry Moscow 86, 361–369 (2021). https://doi.org/10.1134/S0006297921030111
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DOI: https://doi.org/10.1134/S0006297921030111