Rubredoxin Oxidase, a New Flavo-Hemo-Protein, Is the Site of Oxygen Reduction to Water by the "Strict Anaerobe" Desulfovibrio gigas

Chen, Liang; Liu, M.-L.; LeGall, Jean; Fareleira, Paula; Santos, Helena; Xavier, António V.

doi:10.1006/bbrc.1993.1595

Cited by 136 publications

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“…Rubredoxins are known to act as electron carriers for various enzymes. Reports have described the involvement of rubredoxins in oxidative stress protection in Desulfovibrio gigas, Desulfovibrio vulgaris, and Treponema pallidum (5,11,13). ENH1 encodes a chloroplast protein with a putative rubredoxin domain that may also function as an electron carrier.…”

Section: Resultsmentioning

confidence: 99%

“…The suggested biochemical role for rubredoxin proteins is to act as a mediator of electron transfer for various enzymes (41). The rubredoxin from Pseudomonas oleovorans has been reported to be involved in the electron transfer pathway for the -hydroxylation of alkanes and fatty acids in the presence of NADH and O 2 (46), whereas the rubredoxin from Desulfovibrio gigas functions as an electron donor to a favohemoprotein, rubredoxin-oxygen oxidoreductase (11).…”

Section: Discussionmentioning

confidence: 99%

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An Enhancer Mutant of Arabidopsis salt overly sensitive 3 Mediates both Ion Homeostasis and the Oxidative Stress Response

Zhu

Koo

et al. 2007

Molecular and Cellular Biology

128

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The myristoylated calcium sensor SOS3 and its interacting protein kinase, SOS2, play critical regulatory roles in salt tolerance. Mutations in either of these proteins render Arabidopsis thaliana plants hypersensitive to salt stress. We report here the isolation and characterization of a mutant called enh1-1 that enhances the salt sensitivity of sos3-1 and also causes increased salt sensitivity by itself. ENH1 encodes a chloroplastlocalized protein with a PDZ domain at the N-terminal region and a rubredoxin domain in the C-terminal part. Rubredoxins are known to be involved in the reduction of superoxide in some anaerobic bacteria. The enh1-1 mutation causes enhanced accumulation of reactive oxygen species (ROS), particularly under salt stress. ROS also accumulate to higher levels in sos2-1 but not in sos3-1 mutants. The enh1-1 mutation does not enhance sos2-1 phenotypes. Also, enh1-1 and sos2-1 mutants, but not sos3-1 mutants, show increased sensitivity to oxidative stress. These results indicate that ENH1 functions in the detoxification of reactive oxygen species resulting from salt stress by participating in a new salt tolerance pathway that may involve SOS2 but not SOS3.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

An Enhancer Mutant of Arabidopsis salt overly sensitive 3 Mediates both Ion Homeostasis and the Oxidative Stress Response

Zhu

Koo

et al. 2007

Molecular and Cellular Biology

128

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“…Moreover, it is unlikely that SuDH functions as a scavenger of 02 when the organism is accidentally exposed to air, because the apparent Km value for 02 was 0.24 mM, which is equivalent to air at 1.4 atm (1 atm = 101.29 kPa) (at 80°C). Interestingly, a rubredoxin:oxygen oxidoreductase was recently purified from the anaerobic bacterium Desulfovibrio gigas (14). It was proposed to function in a membrane-bound electron transfer chain which leads to energy conservation upon exposure of the organism to 02 (although the affinity of the enzyme for 02 was not reported).…”

Section: Resultsmentioning

confidence: 99%

Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur

1994

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Pyrococcus furiosus is an anaerobic archaeon that grows optimally at 1000C by the fermentation of carbohydrates yielding acetate, C02, and H2 as the primary products. If elemental sulfur (SO) or polysulfide is added to the growth medium, H2S is also produced. The cytoplasmic hydrogenase of P. furiosus, which is responsible for H2 production with ferredoxin as the electron donor, has been shown to also catalyze the reduction of polysulfide to H2S (K. Ma, R. N. Schicho (33). The majority are strict anaerobes, and most are obligately dependent upon the reduction of elemental sulfur (S) to H2S for optimal growth. Molecular H2 or organic compounds serve as electron donors for the apparent respiration of So. Some of the heterotrophic species are able to grow in the absence of S by fermentation-type metabolisms that result in the production of H2. In such cases, the addition of So to the growth medium leads to H2S production and growth stimulation. Since the hyperthermophiles are the most slowly evolving of known life forms, it has been suggested that S0 respiration may represent one of the earliest mechanisms of energy conservation from an evolutionary perspective (40, 47).The mechanisms by which hyperthermophilic organisms reduce So to H2S and the natures of the enzymes involved are far from clear. The situation is complicated by the fact that the abiotic reduction of S0 can also occur at the growth temperatures of these organisms (9). Also, because of the low solubility of S in aqueous media, golysulfide is thought to be the true substrate for microbial S reduction (9,40,41 nism of H2S production from S0 has been investigated in only one autotrophic hyperthermophile, Pyrodictium brockii, an obligate S-reducing species which grows optimally at 1050C. This organism was shown to have a primitive membrane-bound electron transport chain for coupling H2 oxidation and S0 reduction (36). The chain contained hydrogenase, a cytochrome, and a novel quinone, but the So-reducing entity was not purified. In fact, there have been few reports on S5 reduction by mesophilic organisms. For example, Zophel and coworkers screened several different So-reducing bacteria for sulfur oxidoreductase activity (50) and the enzyme responsible in "Spirillum" strain 5175 (44) was postulated to be an iron-sulfur protein possibly associated with a c-type cytochrome (51). However, only one S0-reducing enzyme has been purified and characterized from a mesophile, that from Wolinella succinogenes (20,21,43), an organism which grows with formate as the electron donor and S0 as the electron acceptor (27). From sequencing analysis, it was postulated that its polysulfide reductase is composed of three subunits and is a molybdopterin-containing iron-sulfur protein (21).We are investigating the So-reducing activities of heterotrophic hyperthermophiles such as P. furiosus (18). This obligate anaerobe grows optimally at 100'C by the fermentation of carbohydrates and peptides in which excess reductant, generated mainly in the form of reduced ferredoxin (2,5,30)...

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“…The first proposed D. gigas defense mechanism against O 2 involved a flavometalloprotein, ROO (8), which accomplishes full oxygen reduction to water by accepting electrons from reduced rubredoxin (Rd). Rd is in turn reduced by NADH:rubredoxin oxidoreductase (7,8).ROO belongs to the flavodiiron protein (FDP) family, whose members are widespread in strict and facultative anaerobic Archaea and Bacteria members, as well as in anaerobic protozoa (1, 29, 30). The resolution of its crystallographic structure (12) revealed that each monomer of this homodimeric protein consists of two structural modules, a C-terminal flavin mononucleotide-binding flavodoxin-like domain and an N-terminal metallo-␤-lactamase-like domain.…”

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confidence: 99%

“…However, there is growing evidence that this organism can survive and probably even profit energetically from transient exposure to oxygen (8,23). Like other isolates from the Desulfovibrio genus, D. gigas has metalbinding enzymes for the detoxification of molecular oxygen (rubredoxin:oxygen oxidoreductase [ROO] and cytochrome bd) (8,23), its reactive species (catalase and superoxide dismutase) (9), and superoxide reductase (34). The first proposed D. gigas defense mechanism against O 2 involved a flavometalloprotein, ROO (8), which accomplishes full oxygen reduction to water by accepting electrons from reduced rubredoxin (Rd).…”

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Desulfovibrio gigas Flavodiiron Protein Affords Protection against Nitrosative Stress In Vivo

et al. 2006

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Desulfovibrio gigas flavodiiron protein (FDP), rubredoxin:oxygen oxidoreductase (ROO), was proposed to be the terminal oxidase of a soluble electron transfer chain coupling NADH oxidation to oxygen reduction. However, several members from the FDP family, to which ROO belongs, revealed nitric oxide (NO) reductase activity. Therefore, the protection afforded by ROO against the cytotoxic effects of NO was here investigated. The NO and oxygen reductase activities of recombinant ROO in vitro were tested by amperometric methods, and the enzyme was shown to effectively reduce NO and O 2 . Functional complementation studies of an Escherichia coli mutant strain lacking the ROO homologue flavorubredoxin, an NO reductase, showed that ROO restores the anaerobic growth phenotype of cultures exposed to otherwise-toxic levels of exogenous NO. Additional studies in vivo using a D. gigas roo-deleted strain confirmed an increased sensitivity to NO of the mutant strain in comparison to the wild type. This effect is more pronounced when using the nitrosating agent S-nitrosoglutathione (GSNO), which effectively impairs the growth of the D. gigas ⌬roo strain. roo is constitutively expressed in D. gigas under all conditions tested. However, real-time reverse transcription-PCR analysis revealed a twofold induction of mRNA levels upon exposure to GSNO, suggesting regulation at the transcription level by NO. The newly proposed role of D. gigas ROO as an NO reductase combined with the O 2 reductase activity reveals a versatility which appears to afford protection to D. gigas at the onset of both oxidative and nitrosative stresses.Desulfovibrio gigas is a sulfate-reducing bacterium considered to be a strict anaerobe. However, there is growing evidence that this organism can survive and probably even profit energetically from transient exposure to oxygen (8,23). Like other isolates from the Desulfovibrio genus, D. gigas has metalbinding enzymes for the detoxification of molecular oxygen (rubredoxin:oxygen oxidoreductase [ROO] and cytochrome bd) (8, 23), its reactive species (catalase and superoxide dismutase) (9), and superoxide reductase (34). The first proposed D. gigas defense mechanism against O 2 involved a flavometalloprotein, ROO (8), which accomplishes full oxygen reduction to water by accepting electrons from reduced rubredoxin (Rd). Rd is in turn reduced by NADH:rubredoxin oxidoreductase (7,8).ROO belongs to the flavodiiron protein (FDP) family, whose members are widespread in strict and facultative anaerobic Archaea and Bacteria members, as well as in anaerobic protozoa (1, 29, 30). The resolution of its crystallographic structure (12) revealed that each monomer of this homodimeric protein consists of two structural modules, a C-terminal flavin mononucleotide-binding flavodoxin-like domain and an N-terminal metallo-␤-lactamase-like domain. More recently, the structure of the FDP from Moorella thermoacetica was also solved (33).Although a role in oxygen reduction was initially assigned to the FDP family, recent reports contributed...

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Rubredoxin Oxidase, a New Flavo-Hemo-Protein, Is the Site of Oxygen Reduction to Water by the "Strict Anaerobe" Desulfovibrio gigas

Cited by 136 publications

References 0 publications

An Enhancer Mutant of Arabidopsis salt overly sensitive 3 Mediates both Ion Homeostasis and the Oxidative Stress Response

An Enhancer Mutant of Arabidopsis salt overly sensitive 3 Mediates both Ion Homeostasis and the Oxidative Stress Response

Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur

Desulfovibrio gigas Flavodiiron Protein Affords Protection against Nitrosative Stress In Vivo

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