Purification and Characterization of an Iron Superoxide Dismutase and a Catalase from the Sulfate-Reducing Bacterium
            <i>Desulfovibrio gigas</i>

Santos, Wagner Gouvêa dos; Pacheco, Isabel; Liu, Ming‐Yih; Teixeira, Miguel; Xavier, António V.; LeGall, Jean

doi:10.1128/jb.182.3.796-804.2000

Cited by 102 publications

(65 citation statements)

References 51 publications

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“…Therefore, sulfate-reducing bacteria must deal with oxidative stress. Some sulfate-reducing bacteria have been shown to contain superoxide dismutases (SODs) and catalases, but other species do not demonstrate the activities expected for these enzymes (15,18,43). The apparent absence of SOD and catalase can be rationalized on the basis that their catalytic dismutation reactions (reactions 1 and 2) generate O 2 , which may be disadvantageous for strict anaerobes.…”

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confidence: 99%

Rubrerythrin and Rubredoxin Oxidoreductase inDesulfovibrio vulgaris: a Novel Oxidative Stress Protection System

et al. 2001

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Evidence is presented for an alternative to the superoxide dismutase (SOD)-catalase oxidative stress defense system in Desulfovibrio vulgaris (strain Hildenborough). This alternative system consists of the nonheme iron proteins, rubrerythrin (Rbr) and rubredoxin oxidoreductase (Rbo), the product of the rbo gene (also called desulfoferrodoxin). A ⌬rbo strain of D. vulgaris was found to be more sensitive to internal superoxide exposure than was the wild type. Unlike Rbo, expression of plasmid-borne Rbr failed to restore the aerobic growth of a SOD-deficient strain of Escherichia coli. Conversely, plasmid-borne expression of two different Rbrs from D. vulgaris increased the viability of a catalase-deficient strain of E. coli that had been exposed to hydrogen peroxide whereas Rbo actually decreased the viability. A previously undescribed D. vulgaris gene was found to encode a protein having 50% sequence identity to that of E. coli Fe-SOD. This gene also encoded an extended N-terminal sequence with high homologies to export signal peptides of periplasmic redox proteins. The SOD activity of D. vulgaris is not affected by the absence of Rbo and is concentrated in the periplasmic fraction of cell extracts. These results are consistent with a superoxide reductase rather than SOD activity of Rbo and with a peroxidase activity of Rbr. A joint role for Rbo and Rbr as a novel cytoplasmic oxidative stress protection system in D. vulgaris and other anaerobic microorganisms is proposed.

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confidence: 99%

Rubrerythrin and Rubredoxin Oxidoreductase inDesulfovibrio vulgaris: a Novel Oxidative Stress Protection System

et al. 2001

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“…The survival of a variety of cultured SRB under oxic to suboxic conditions has been explained on the basis of enzymes that may aid in reducing the impact of toxic oxygen species, such as superoxide and hydrogen peroxide. Several SRB possess catalase and superoxide dismutase activities (25,34), as well as a variety of other enzymes and cofactors that may be involved in neutralizing toxic oxygen species (1,54,83,84). The mechanisms by which sulfate reduction may occur in oxic environments are not as clear, although several possible mechanisms have been proposed.…”

Section: Discussionmentioning

confidence: 99%

Sulfate-Reducing Bacteria in Tubes Constructed by the Marine Infaunal Polychaete Diopatra cuprea

Matsui

Ringelberg

Lovell

2004

Appl Environ Microbiol

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Marine infaunal burrows and tubes greatly enhance solute transport between sediments and the overlying water column and are sites of elevated microbial activity. Biotic and abiotic controls of the compositions and activities of burrow and tube microbial communities are poorly understood. The microbial communities in tubes of the marine infaunal polychaete Diopatria cuprea collected from two different sediment habitats were examined. The bacterial communities in the tubes from a sandy sediment differed from those in the tubes from a muddy sediment. The difference in community structure also extended to the sulfate-reducing bacterial (SRB) assemblage, although it was not as pronounced for this functional group of species. PCR-amplified 16S rRNA gene sequences recovered from Diopatra tube SRB by clonal library construction and screening were all related to the family Desulfobacteriaceae. This finding was supported by phospholipid fatty acid analysis and by hybridization of 16S rRNA probes specific for members of the genera Desulfosarcina, Desulfobacter, Desulfobacterium, Desulfobotulus, Desulfococcus, and Desulfovibrio and some members of the genera Desulfomonas, Desulfuromonas, and Desulfomicrobium with 16S rRNA gene sequences resolved by denaturing gradient gel electrophoresis. Two of six SRB clones from the clone library were not detected in tubes from the sandy sediment. The habitat in which the D. cuprea tubes were constructed had a strong influence on the tube bacterial community as a whole, as well as on the SRB assemblage.

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“…As a matter of fact, cells contain a number of potential generators of superoxide anion, such as cytochrome, flavodoxin, and ferredoxin. Superoxide dismutase and catalase, which are enzymes well known to eliminate superoxide and hydrogen peroxide in aerobic organisms, have also been characterized in some Desulfovibrio species (17,18). In addition to these enzymes, a superoxide reductase (SOR) and a rubrerythrin, which has an NADH-dependent H 2 O 2 reductase activity, have also been found in sulfate-reducing bacteria (19 -22).…”

Section: Sulfate-reducing Bacteria Like Desulfovibrio Vulgarismentioning

confidence: 99%

A New Function of the Desulfovibrio vulgaris Hildenborough [Fe] Hydrogenase in the Protection against Oxidative Stress

Fournier

Dermoun

Durand

et al. 2004

Journal of Biological Chemistry

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Sulfate-reducing bacteria, like Desulfovibrio vulgarisHildenborough, have developed a set of reactions allowing them to survive in oxic environments and even to reduce molecular oxygen to water. D. vulgaris contains a cytoplasmic superoxide reductase (SOR) and a periplasmic superoxide dismutase (SOD) involved in the elimination of superoxide anions. To assign the function of SOD, the periplasmic [Fe] hydrogenase activity was followed in both wild-type and sod deletant strains. This activity was lower in the strain lacking the SOD than in the wild-type when the cells were exposed to oxygen for a short time. The periplasmic SOD is thus involved in the protection of sensitive iron-sulfur-containing enzyme against superoxide-induced damages. Surprisingly, production of the periplasmic Microbial sulfate reduction has been reported to be an ancient process as old as 3.47 gigayears. Sulfate reduction thus represents an early specific metabolic pathway, allowing time calibration of a deep node on the tree of life (1). Sulfate-reducing bacteria (SRB) 1 are universally distributed in marine and microbial mats where sulfate reduction is the dominant anaerobic biomineralization pathway. They constitute a group of anaerobic prokaryotes, which are unified by sharing the capacity to carry out dissimilatory sulfate reduction to sulfide as a major component of their bioenergetic processes. Although sulfate reduction is generally considered to be an anaerobic process, the abundance and metabolic activity of SRB in oxic zones is frequently evaluated as higher than those in neighboring anoxic zones in numerous biotopes (2, 3). In situ detection of sulfate reducing activity and SRB populations in these biotopes showed that SRB species did not have the same capability of resisting oxygen. Analysis of the photooxic zone of cyanobacterial mats revealed a well-defined SRB distribution. Although Desulfobacter and Desulfobacterium were restricted to the deepest levels in the mats, Desulfococcus were predominant in the photooxic zone with Desulfovibrio also present. This distribution suggests that both groups contain oxygen-tolerant members (4). It is thus clear that SRB exhibit a differentiated set of reactions to oxygen: first, many SRB form aggregates (5), resulting in a higher tolerance to oxygen exposure; second, at least Desulfovibrio species migrate in response to the oxygen concentration in their environment (5); and third, many species respire with oxygen (6). However, although it has been demonstrated that aerobic respiration is coupled with proton translocation and ATP conservation, aerobic growth in pure culture has never been proved (7). The high respiration rate merely seems to have a protective function. In an oxygen gradient, bacteria form bands at the outer edge of the oxic zone, suggesting both negative and positive aerotaxis responses (8). The capability of SRB to move toward oxygen and reduce it might play an ecological role in the zone of transition from an oxic to an anoxic environment, protecting themselves and other...

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Purification and Characterization of an Iron Superoxide Dismutase and a Catalase from the Sulfate-Reducing Bacterium Desulfovibrio gigas

Cited by 102 publications

References 51 publications

Rubrerythrin and Rubredoxin Oxidoreductase inDesulfovibrio vulgaris: a Novel Oxidative Stress Protection System

Rubrerythrin and Rubredoxin Oxidoreductase inDesulfovibrio vulgaris: a Novel Oxidative Stress Protection System

Sulfate-Reducing Bacteria in Tubes Constructed by the Marine Infaunal Polychaete Diopatra cuprea

A New Function of the Desulfovibrio vulgaris Hildenborough [Fe] Hydrogenase in the Protection against Oxidative Stress

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