1887

Abstract

The utilization of organosulfonates as carbon sources by aerobic or nitrate-reducing bacteria usually involves a measurable, uncharacterized sulfite dehydrogenase. This is tacitly assumed to be sulfite : ferricytochrome- oxidoreductase [EC 1.8.2.1], despite negligible interaction with (eukaryotic) cytochrome : the enzyme is assayed at high specific activity with ferricyanide as electron acceptor. Purified periplasmic sulfite dehydrogenases (SorAB, SoxCD) are known from chemoautotrophic growth and are termed ‘sulfite oxidases’ by bioinformatic services. The catalytic unit (SorA, SoxC; termed ‘sulfite oxidases’ cd02114 and cd02113, respectively) binds a molybdenum-cofactor (Moco), and involves a cytochrome (SorB, SoxD) as electron acceptor. The genomes of several bacteria that express a sulfite dehydrogenase during heterotrophic growth contain neither nor genes; others contain at least four paralogues, for example H16, which is known to express an inducible sulfite dehydrogenase during growth with taurine (2-aminoethanesulfonate). This soluble enzyme was enriched 320-fold in four steps. The 40 kDa protein (denatured) had an -terminal amino acid sequence which started at position 42 of the deduced sequence of H16_B0860 (termed ‘sulfite oxidase’ cd02114), which we named SorA. The neighbouring gene is an orthologue of , and the genes were co-transcribed. Cell fractionation showed SorA to be periplasmic. The corresponding enzyme in SPH-1 was enriched 270-fold, identified as Daci_0055 (termed ‘sulfite oxidase’ cd02110) and has a cytochrome encoded downstream. We presume, from genomic data for bacteria and archaea, that there are several subgroups of sulfite dehydrogenases, which all contain a Moco, and transfer electrons to a specific cytochrome .

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2008-01-01
2019-11-16
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vol. , part 1, pp. 256 - 263

Desulfonative organisms with sequenced genomes and the candidate loci to encode enzymes which bind the molybendum cofactor (Moco) [ PDF] (23 kb)



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