NADH Peroxidase Activity of Rubrerythrin

Coulter, Eric D.; Shenvi, Neeta; Kurtz, Donald M.

doi:10.1006/bbrc.1999.0197

Cited by 83 publications

(94 citation statements)

References 21 publications

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“…AAB39991-1) and to other rubrerythrins from strictly anaerobic bacteria and archaea. The rubrerythrin and related nigerythrin protein from the anaerobic sulphatereducing bacterium D. vulgaris are suspected to possess NADH peroxidase activity at least in an in vitro assay system (Coulter et al, 1999).…”

Section: Resultsmentioning

confidence: 99%

“…perfringens 13R possesses three genes encoding a nonhaem iron protein belonging to the rubrerythrin family. Some members of this family possess NADH peroxidase activity in an in vitro system containing NADH and H 2 O 2 , and a bacterial NADH oxidoreductase (Coulter et al, 1999). However, the specific activity is very low and the activity detected in vitro may be different from that expressed in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…On: Fri, 11 May 2018 10:57:58 Lumppio et al, 1997;Voordouw & Voordouw, 1998;Coulter et al, 1999;Jenney et al, 1999;Lumppio et al, 2001;Emerson et al, 2002). Homologues of some of the oxidative stress response genes found in Desulfovibrio vulgaris have thus been sought in C. perfringens.…”

Section: Introductionmentioning

confidence: 99%

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Oxidative stress response in Clostridium perfringens

2004

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Clostridium perfringens, a strictly anaerobic bacterium, is able to survive when exposed to oxygen for short periods of time and exhibits a complex adaptive response to reactive oxygen species, both under aerobic and anaerobic conditions. However, this adaptive response is not completely understood. C. perfringens possesses specialized genes that might be involved in this adaptive process, such as those encoding superoxide dismutase (SOD), superoxide reductase and alkyl hydroperoxide reductase, but their contribution to the oxidative stress response and their control mechanisms are unknown. By a combination of functional complementation of Escherichia coli strains impaired in either SOD, alkyl hydroperoxide reductase (AhpC) or catalase activity (Cat), transcription analysis and characterization of mutants impaired in regulatory genes, it was concluded that: (i) the product of the sod gene is certainly essential to scavenge superoxide radicals, (ii) the ahpC gene, which is fully induced in all oxidative stress conditions, is probably involved in the scavenging of all intracellular peroxides, (iii) the three rubrerythrin (rbr) genes of C. perfringens do not encode proteins with in vivo H 2 O 2 reductase activity, and (iv) the two rubredoxin (rub) genes do not contribute to the hypothetical superoxide reductase activity, but are likely to belong to an electron transfer chain involved in energy metabolism.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Oxidative stress response in Clostridium perfringens

2004

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“…We have found that P. gingivalis possesses a Dps-like protein (data not shown). Another candidate is rubrerythrin, which is a member of the ferritin\bacterioferritin\rubrerythrin superfamily and has thus far been found only in ' anaerobic ' bacteria (Andrews, 1998 ;Lehmann et al, 1996 ;Bonomi et al, 1996 ;Coulter et al, 1999). In fact, a gene encoding rubrerythrin has been identified in the partial genome sequence of P. gingivalis (http :\\www.tigr.org).…”

Section: Discussionmentioning

confidence: 99%

Ferritin from the obligate anaerobe Porphyromonas gingivalis: purification, gene cloning and mutant studies The GenBank accession number for the sequence reported in this paper is AB016086.

et al. 2000

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Porphyromonas gingivalis is an obligate anaerobe that utilizes haem, transferrin and haemoglobin efficiently as sources of iron for growth, and has the ability to store haem on its cell surface, resulting in black pigmentation of colonies on blood agar plates. However, little is known about intracellular iron storage in this organism. Ferritin is one of the intracellular iron-storage proteins and may also contribute to the protection of organisms against oxidative stresses generated by intracellular free iron. A ferritin-like protein was purified from P. gingivalis and the encoding gene (ftn) was cloned from chromosomal DNA using information on its amino-terminal amino acid sequence. Comparison of the amino acid sequence deduced from the nucleotide sequence of ftn with those of known ferritins and bacterioferritins identified the protein as a ferritin and positioned it between proteins from the Proteobacteria and Thermotogales. The P. gingivalis ferritin was found to contain non-haem iron, thus confirming its identity. Construction and characterization of a P. gingivalis ferritin-deficient mutant revealed that the ferritin was particularly important for the bacterium to survive under irondepleted conditions (both haemin and transferrin starvation), indicating that intracellular iron is stored in ferritin regardless of the iron source and that the iron stored in ferritin is utilized under iron-restricted conditions. However, the ferritin appeared not to contribute to protection against oxidative stresses caused by peroxides and atmospheric oxygen.

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“…Two disproportionating enzymes, the superoxide dismutase (Sod) and catalase (Kat), are broadly distributed in SRB (Hatchikian and Henry 1977;dos Santos et al 2000;Fournier et al 2003). The superoxide reductases (Sor) and rubrerythrins catalyzing the reductive elimination of superoxide and hydrogen peroxide, respectively, are also present in these organisms (Pierik et al 1993;Voordouw and Voordouw 1998;Coulter et al 1999;Lombard et al 2000). Two structurally different types of Sor are found in SRB, the rubredoxin oxidoreductase (Rbo) (also named desulfoferredoxin) (Moura et al 1990;Voordouw and Voordouw 1998;Lombard et al 2000) and neelaredoxin (Abreu et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional response of Desulfovibrio vulgaris Hildenborough to oxidative stress mimicking environmental conditions

Pereira

Xavier

et al. 2007

Arch Microbiol

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Sulphate-reducing bacteria are anaerobes readily found in oxic-anoxic interfaces. Multiple defence pathways against oxidative conditions were identified in these organisms and proposed to be differentially expressed under different concentrations of oxygen, contributing to their ability to survive oxic conditions. In this study, Desulfovibrio vulgaris Hildenborough cells were exposed to the highest concentration of oxygen that sulphate-reducing bacteria are likely to encounter in natural habitats, and the global transcriptomic response was determined. 307 genes were responsive, with cellular roles in energy metabolism, protein fate, cell envelope and regulatory functions, including multiple genes encoding heat shock proteins, peptidases and proteins with heat shock promoters. Of the oxygen reducing mechanisms of D. vulgaris only the periplasmic hydrogen-dependent mechanism is up-regulated, involving the [NiFeSe] hydrogenase, formate dehydrogenase(s) and the Hmc membrane complex. The oxidative defence response concentrates on damage repair by metal-free enzymes. . These data, together with the down regulation of the Fur operon, which restricts the availability of iron, and the lack of response of the PerR operon, suggest that a major effect of this oxygen stress is the inactivation and/or degradation of multiple metalloproteins present in D. vulgaris as a consequence of oxidative damage to their metal clusters.

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NADH Peroxidase Activity of Rubrerythrin

Cited by 83 publications

References 21 publications

Oxidative stress response in Clostridium perfringens

Oxidative stress response in Clostridium perfringens

Ferritin from the obligate anaerobe Porphyromonas gingivalis: purification, gene cloning and mutant studies The GenBank accession number for the sequence reported in this paper is AB016086.

Transcriptional response of Desulfovibrio vulgaris Hildenborough to oxidative stress mimicking environmental conditions

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