Abstract
The requirement of MobA for molybdoenzymes with different molybdenum cofactors was analyzed in Rhodobacter capsulatus. MobA is essential for DMSO reductase and nitrate reductase activity, both enzymes containing the molybdopterin guanine dinucleotide cofactor (MGD), but not for active xanthine dehydrogenase, harboring the molybdopterin cofactor. In contrast to the mob locus of Escherichia coli and R. sphaeroides, the mobB gene is not located downstream of mobA in R. capsulatus. The mobA gene is expressed constitutively at low levels and no increase in mobA expression could be observed even under conditions of high MGD demand.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Blotting, Southern
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Chromosome Mapping
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Coenzymes / chemistry
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Coenzymes / metabolism*
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DNA, Bacterial
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Escherichia coli Proteins*
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Gene Expression Regulation, Bacterial
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Guanine Nucleotides / metabolism*
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Iron-Sulfur Proteins*
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Metalloproteins / metabolism*
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Molecular Sequence Data
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Molybdenum / metabolism*
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Molybdenum Cofactors
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Mutagenesis, Insertional
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Nitrate Reductase
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Nitrate Reductases / chemistry
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Nitrate Reductases / metabolism
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Oxidoreductases / chemistry
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Oxidoreductases / metabolism
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Pteridines / metabolism*
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Pterins / metabolism*
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Rhodobacter capsulatus / enzymology*
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Rhodobacter capsulatus / genetics
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Sulfurtransferases / metabolism
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Xanthine Dehydrogenase / chemistry
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Xanthine Dehydrogenase / metabolism
Substances
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Bacterial Proteins
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Coenzymes
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DNA, Bacterial
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Escherichia coli Proteins
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Guanine Nucleotides
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Iron-Sulfur Proteins
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Metalloproteins
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Molybdenum Cofactors
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Pteridines
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Pterins
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mobA protein, E coli
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molybdopterin guanine dinucleotide
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Molybdenum
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molybdenum cofactor
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Oxidoreductases
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Xanthine Dehydrogenase
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Nitrate Reductases
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Nitrate Reductase
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dimethyl sulfoxide reductase
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Sulfurtransferases
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molybdopterin synthase