Periplasmic oxygen reduction by Desulfovibrio species

Baumgarten, Antje; Redenius, Insa; Kranczoch, Jan; Cypionka, Heribert

doi:10.1007/s002030100329

Cited by 50 publications

(32 citation statements)

References 30 publications

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“…In Desulfovibrio species, the highest oxygenuptake activity is found in the periplasmic fraction, with H 2 as electron donor. Cytochrome c 3 was found to play a major role in oxygen reduction [42,43].…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Mander¹,

Duin²,

Linder³

et al. 2002

Eur J Biochem

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Mander¹,

Duin²,

Linder³

et al. 2002

Eur J Biochem

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“…In the case of homoacetogenic bacteria isolated from termite guts, hydrogen oxidation was shown to be a way to remove O 2 from the environment (6). A role in a protective mechanism against oxidative stress was proposed for a periplasmic FeFe hydrogenase of the deltaproteobacterium Desulfovibrio vulgaris (5,16).…”

Section: H Ydrogenases Are Ubiquitous Enzymes Catalyzing the Reversibmentioning

confidence: 99%

Role of the NiFe Hydrogenase Hya in Oxidative Stress Defense in Geobacter sulfurreducens

Tremblay

Lovley

2012

J Bacteriol

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Geobacter sulfurreducens , an Fe(III)-reducing deltaproteobacterium found in anoxic subsurface environments, contains 4 NiFe hydrogenases. Hyb, a periplasmically oriented membrane-bound NiFe hydrogenase, is essential for hydrogen-dependent growth. The functions of the three other hydrogenases are unknown. We show here that the other periplasmically oriented membrane-bound NiFe hydrogenase, Hya, is necessary for growth after exposure to oxidative stress when hydrogen or a highly limiting concentration of acetate is the electron source. The beneficial impact of Hya on growth was dependent on the presence of H 2 in the atmosphere. Moreover, the Hya-deficient strain was more sensitive to the presence of superoxide or hydrogen peroxide. Hya was also required to safeguard Hyb hydrogen oxidation activity after exposure to O 2 . Overexpression studies demonstrated that Hya was more resistant to oxidative stress than Hyb. Overexpression of Hya also resulted in the creation of a recombinant strain better fitted for exposure to oxidative stress than wild-type G. sulfurreducens . These results demonstrate that one of the physiological roles of the O 2 -resistant Hya is to participate in the oxidative stress defense of G. sulfurreducens .

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“…Genome analysis of D. vulgaris Hildenborough (www.tigr.org) and D. desulfuricans G20 (www.jgi.doe.gov) revealed the presence of both genes for cytochrome c oxidase and cytochrome bd. The involvement of hydrogenase and c-type cytochromes in periplasmic oxygen reduction by Desulfovibrio species was recently proposed (13). Although these two classes of metalloproteins have been shown to be the key enzymes of the energy-generating metabolism in anaerobic sulfate respiration (14), oxygen reduction constitutes a new mechanism in which these two proteins might be involved.…”

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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Periplasmic oxygen reduction by Desulfovibrio species

Cited by 50 publications

References 30 publications

Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Role of the NiFe Hydrogenase Hya in Oxidative Stress Defense in Geobacter sulfurreducens

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

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