Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli

Pierson, Dorothy E.; Campbell, A

doi:10.1128/jb.172.4.2194-2198.1990

Cited by 73 publications

(48 citation statements)

References 38 publications

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“…The possibility that one of these modes in the reduced sample arises from Mo-OH 2 stretching was ruled out by the absence of any significant isotope shift for samples exchanged into H 2 18 O buffer (data not shown). In Me 2 SO reductase, Mo-O(Ser) stretching modes were tentatively assigned to bands at 536 and 513 cm Ϫ1 in the Mo(VI) and Mo(IV) forms, respectively (12). This assignment has recently been supported by the loss of these bands upon mutation of Ser-147 to a cysteine residue in Me 2 SO reductase (26).…”

Section: Resultsmentioning

confidence: 90%

“…2). Although the precise role for BSO reductase in bacterial metabolism has yet to be defined, potential physiological functions include scavenging biotin sulfoxide from the environment, reducing bound intracellular biotin that has become oxidized in an aerobic environment, and protecting the cell from oxidative damage (12). Extensive characterization of this enzyme has been limited due to the low natural abundance of the protein and its constitutive expression (13).…”

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confidence: 99%

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Resonance Raman Characterization of Biotin Sulfoxide Reductase

Garton

Temple

Dhawan

et al. 2000

Journal of Biological Chemistry

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Resonance Raman spectroscopy has been used to define active site structures for oxidized Mo(VI) and reduced Mo(IV) forms of recombinant Rhodobacter sphaeroides biotin sulfoxide reductase expressed in Escherichia coli. On the basis of 18 With the exception of nitrogenase, molybdenum enzymes catalyze formal oxygen atom transfer between water and substrate and contain an active site in which the molybdenum is coordinated by the dithiolene side chain of one or two molybdopterins (Fig. 1a) (1-3). Although the recent proliferation of x-ray crystal structures for mononuclear molybdenum enzymes has revealed a common structure for the molybdopterin cofactor, they have also revealed considerable diversity in the molybdenum coordination environment (2-11). However, on the basis of the available crystallographic, spectroscopic, primary sequence, and cyanide inhibition data, these enzymes can be divided into three large families (Fig. 1b) (1). Hydroxylases, such as Desulfovibrio gigas aldehyde oxidoreductase, xanthine oxidase, and xanthine dehydrogenase, represent the xanthine oxidase family, characterized by a Mo(VI) active site with a single molybdopterin, as well as terminal oxo and sulfido groups. The oxotransferase class of molybdoenzymes catalyzes direct oxygen atom transfer between substrate and water and can be divided into two families. The sulfite oxidase family, as represented by sulfite oxidase and assimilatory nitrate reductase, contains Mo(VI) ligated by two oxo groups in addition to a single molybdopterin and a cysteine residue. The dimethyl sulfoxide (Me 2 SO) reductase family comprises mono-oxoMo(VI) sites ligated by two molybdopterins and a protein side chain ligand such as serine, cysteine, or selenocysteine. In addition to Me 2 SO reductase, this family also includes formate dehydrogenase, dissimilatory nitrate reductase, and biotin sulfoxide (BSO) 1 reductase. BSO reductase is found in bacterial systems, such as Rhodobacter sphaeroides and Escherichia coli, and catalyzes the reduction of d-biotin d-sulfoxide to d-biotin (Fig. 2). Although the precise role for BSO reductase in bacterial metabolism has yet to be defined, potential physiological functions include scavenging biotin sulfoxide from the environment, reducing bound intracellular biotin that has become oxidized in an aerobic environment, and protecting the cell from oxidative damage (12). Extensive characterization of this enzyme has been limited due to the low natural abundance of the protein and its constitutive expression (13). However, R. sphaeroides BSO reductase has recently been heterologously expressed in E. coli and characterized as containing the molybdopterin guanine dinucleotide form of the molybdopterin cofactor (14). Using either reduced methyl viologen or NADPH as electron donor, the enzyme was found to exhibit broad substrate specificity and was able to catalyze reduction of nicotinamide-N-oxide, methionine sulfoxide, trimethylamine-N-oxide, and dimethyl sulfoxide with varying efficiencies, in addition to the reduction of biotin ...

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Section: Resultsmentioning

confidence: 90%

mentioning

confidence: 99%

Resonance Raman Characterization of Biotin Sulfoxide Reductase

Garton

Temple

Dhawan

et al. 2000

Journal of Biological Chemistry

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“…Genes which show increased transcriptional levels (Table 2) also have some commonality between strains. Some induced genes have a functional association with metal cations, including nikD [Ni(II) export ; Navarro et al, 1993], yfeC [putative chelated-Fe(II) export ; Bearden et al, 1998], yeaJ (shows sequence similarity to hmsT, a putative regulator of haem storage ; Jones et al, 1999) and bisC (biotin sulfoxide reductase, binds molybdenum ; Pierson & Campbell, 1990). These gene products could be involved in the chelation of excess cytosolic metal ions which may generate tolerance or perhaps represent compensatory alterations which preserve cation [e.g.…”

Section: Genementioning

confidence: 99%

Metal-ion tolerance in Escherichia coli: analysis of transcriptional profiles by gene-array technology

Brocklehurst

Morby

2000

Microbiology

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Escherichia coli was adapted to grow in medium containing substantially elevated concentrations of either Zn(II), Cd(II), Co(II) or Ni(II). Whole-genome transcriptional profiles were generated from adapted strains and analysed for significant alteration in transcript abundance with reference to a wild-type strain. Similar alterations in specific message levels were observed for strains adapted to the four metal ions. One unexpected trend was the increase in transcript level of genes involved in transposition of IS elements, particularly insA. Subsequent expression of insA-7 from a heterologous promoter in E. coli conferred tolerance to Zn(II).

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“…Although DMSOR also functions as a terminal enzyme during anaerobic respiration, it is able to utilize a greater variety of substrates including Me 3 NO and dimethyl sulfoxide (Me 2 SO) (21). BSOR, a cytoplasmic protein whose possible roles include scavenging biotin sulfoxide (BSO) to generate biotin and protecting the cell from oxidative damage (22), has also been shown to use a variety of S-and N-oxides (23).…”

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confidence: 99%

An Active Site Tyrosine Influences the Ability of the Dimethyl Sulfoxide Reductase Family of Molybdopterin Enzymes to Reduce S-Oxides

Johnson

Rajagopalan

2001

Journal of Biological Chemistry

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Dimethyl sulfoxide reductase (DMSOR), trimethylamine-N-oxide reductase (TMAOR), and biotin sulfoxide reductase (BSOR) are members of a class of bacterial oxotransferases that contain the bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The presence of a Tyr residue in the active site of DMSOR and BSOR that is missing in TMAOR has been implicated in the inability of TMAOR, unlike DMSOR and BSOR, to utilize S-oxides. To test this hypothesis, Escherichia coli TMAOR was cloned and expressed at high levels, and site-directed mutagenesis was utilized to generate the Tyr-114 3 Ala and Phe variants of Rhodobacter sphaeroides DMSOR and insert a Tyr residue into the equivalent position in TMAOR. Although all of the mutants turn over in a manner similar to their respective wildtype enzymes, mutation of Tyr-114 in DMSOR results in a decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide (Me 3 NO), with a greater change observed for DMSOR-Y114A. Insertion of a Tyr into TMAOR results in a decreased preference for Me 3 NO relative to dimethyl sulfoxide. Kinetic analysis and UV-visible absorption spectra indicate that the ability of DMSOR to be reduced by dimethyl sulfide is lost upon mutation of Tyr-114 and that TMAOR does not exhibit this activity even in the Tyr insertion mutant.

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Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli

Cited by 73 publications

References 38 publications

Resonance Raman Characterization of Biotin Sulfoxide Reductase

Resonance Raman Characterization of Biotin Sulfoxide Reductase

Metal-ion tolerance in Escherichia coli: analysis of transcriptional profiles by gene-array technology

An Active Site Tyrosine Influences the Ability of the Dimethyl Sulfoxide Reductase Family of Molybdopterin Enzymes to Reduce S-Oxides

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