Wolinella succinogenes nitrite reductase: Purification and properties

Liu, M

doi:10.1016/0378-1097(83)90060-5

Cited by 10 publications

(23 citation statements)

References 7 publications

(9 reference statements)

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“…A fifth haem C group is probably linked to the CxxCK motif. The molecular mass of W. succinogenes NrfA, including the five haem C groups, is calculated to be 58 kDa, in fair agreement with the apparent molecular mass obtained from SDS–PAGE (Liu et al ., 1983; Schröder et al ., 1985; Schumacher et al ., 1994).…”

Section: Resultsmentioning

confidence: 99%

“…W. succinogenes cells grown with nitrate contain nitrite reductase activity in the membrane as well as in the soluble cell fraction (Liu et al ., 1983; Schröder et al ., 1985; Schumacher et al ., 1994). The soluble nitrite reductase was proposed to be identical to the catalytic subunit (NrfA) of the membrane‐bound enzyme.…”

Section: Resultsmentioning

confidence: 99%

“…The membrane fraction was found to catalyse the reduction of nitrite to NH 4 + by reduced viologens, and this activity was not abolished upon MK extraction (Schröder et al ., 1985). Isolation of the corresponding enzyme led to a cytochrome c with the properties of the nitrite reductase isolated from the soluble cell fraction of W. succinogenes (Liu et al ., 1983). The enzyme prepared from the membrane fraction could be incorporated into liposomes together with hydrogenase and vitamin K 1 (Schröder et al ., 1985).…”

Section: Introductionmentioning

confidence: 99%

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A NapC/NirT‐type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes

Simon

Groß

Einsle

et al. 2000

Molecular Microbiology

145

190

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Wolinella succinogenes can grow by anaerobic respiration with nitrate or nitrite using formate as electron donor. Two forms of nitrite reductase were isolated from the membrane fraction of W. succinogenes. One form consisted of a 58 kDa polypeptide (NrfA) that was identical to the periplasmic nitrite reductase. The other form consisted of NrfA and a 22 kDa polypeptide (NrfH). Both forms catalysed nitrite reduction by reduced benzyl viologen, but only the dimeric form catalysed nitrite reduction by dimethylnaphthoquinol. Liposomes containing heterodimeric nitrite reductase, formate dehydrogenase and menaquinone catalysed the electron transport from formate to nitrite; this was coupled to the generation of an electrochemical proton potential (positive outside) across the liposomal membrane. It is concluded that the electron transfer from menaquinol to the catalytic subunit (NrfA) of W. succinogenes nitrite reductase is mediated by NrfH. The structural genes nrfA and nrfH were identified in an apparent operon (nrfHAIJ) with two additional genes. The gene nrfA encodes the precursor of NrfA carrying an N‐terminal signal peptide (22 residues). NrfA (485 residues) is predicted to be a hydrophilic protein that is similar to the NrfA proteins of Sulfurospirillum deleyianum and of Escherichia coli. NrfH (177 residues) is predicted to be a membrane‐bound tetrahaem cytochrome c belonging to the NapC/NirT family. The products of nrfI and nrfJ resemble proteins involved in cytochrome c biogenesis. The C‐terminal third of NrfI (902 amino acid residues) is similar to CcsA proteins from Gram‐positive bacteria, cyanobacteria and chloroplasts. The residual N‐terminal part of NrfI resembles Ccs1 proteins. The deduced NrfJ protein resembles the thioredoxin‐like proteins (ResA) of Helicobacter pylori and of Bacillus subtilis, but lacks the common motif CxxC of ResA. The properties of three deletion mutants of W. succinogenes (ΔnrfJ,ΔnrfIJ and ΔnrfAIJ) were studied. Mutants ΔnrfAIJ and ΔnrfIJ did not grow with nitrite as terminal electron acceptor or with nitrate in the absence of NH4+ and lacked nitrite reductase activity, whereas mutant ΔnrfJ showed wild‐type properties. The NrfA protein formed by mutant ΔnrfIJ seemed to lack part of the haem C, suggesting that NrfI is involved in NrfA maturation.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A NapC/NirT‐type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes

Simon

Groß

Einsle

et al. 2000

Molecular Microbiology

145

190

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“…Many sulfate reducing Deltaproteobacteria are able to perform DNRA in the presence of nitrate (Dannenberg et al, 1992;Mitchell et al, 1986;Pereira et al, 1996;Seitz and Cypionka, 1986) although there has been recent evidence that sulfate reduction is preferred over DNRA if both electron acceptors are present (Marietou et al, 2009). NrfA has been purified and characterized from many different organisms as for example Escherichia coli (Kajie and Anraku, 1986;, Desulfovibrio desulfuricans , Wolinella succinogenes (Blackmore et al, 1986;Liu et al, 1983) and Vibrio fischeri (Liu et al, 1988). In other cases, the corresponding enzymes have only been predicted from the nrf genes detected in genome sequences and their structural and functional characterization remains the task of further research.…”

Section: Dissimilatory Nitrate Reduction To Ammonium (Dnra)mentioning

confidence: 99%

Microbial nitrate respiration – Genes, enzymes and environmental distribution

Kraft

Strous

Tegetmeyer

2011

Journal of Biotechnology

367

252

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“…It was first isolated in 1981 from the sulfate‐reducing bacterium Desulfovibrio desulfuricans ATCC 27774 [3], when grown anaerobically in nitrate, instead of sulfate. Since then, a number of respiratory ammonia‐forming ccNiRs have been isolated from several nitrate‐grown bacteria as Escherichia coli K‐12 [4], Vibrio alginolyticus [5], Vibrio fisheri [6], Wolinella succinogenes [7] and Sulfurospirillum deleyianum [8]. Although not completely characterized, the iron‐reducing bacterium Geobacter metallireducens also exhibits cytochrome c nitrite reductase activity [9].…”

mentioning

confidence: 99%

The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774

Almeida

Macieira

Gonçalves

et al. 2003

European Journal of Biochemistry

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The cytochrome c nitrite reductase is isolated from the membranes of the sulfate‐reducing bacterium Desulfovibrio desulfuricans ATCC 27774 as a heterooligomeric complex composed by two subunits (61 kDa and 19 kDa) containing c‐type hemes, encoded by the genes nrfA and nrfH, respectively. The extracted complex has in average a 2NrfA:1NrfH composition. The separation of ccNiR subunits from one another is accomplished by gel filtration chromatography in the presence of SDS. The amino‐acid sequence and biochemical subunits characterization show that NrfA contains five hemes and NrfH four hemes. These considerations enabled the revision of a vast amount of existing spectroscopic data on the NrfHA complex that was not originally well interpreted due to the lack of knowledge on the heme content and the oligomeric enzyme status. Based on EPR and Mössbauer parameters and their correlation to structural information recently obtained from X‐ray crystallography on the NrfA structure [Cunha, C.A., Macieira, S., Dias, J.M., Almeida, M.G., Gonçalves, L.M.L., Costa, C., Lampreia, J., Huber, R., Moura, J.J.G., Moura, I. & Romão, M. (2003) J. Biol. Chem. 278, 17455–17465], we propose the full assignment of midpoint reduction potentials values to the individual hemes. NrfA contains the high‐spin catalytic site (−80 mV) as well as a quite unusual high reduction potential (+150 mV)/low‐spin bis‐His coordinated heme, considered to be the site where electrons enter. In addition, the reassessment of the spectroscopic data allowed the first partial spectroscopic characterization of the NrfH subunit. The four NrfH hemes are all in a low‐spin state (S = 1/2). One of them has a gmax at 3.55, characteristic of bis‐histidinyl iron ligands in a noncoplanar arrangement, and has a positive reduction potential.

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Wolinella succinogenes nitrite reductase: Purification and properties

Cited by 10 publications

References 7 publications

A NapC/NirT‐type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes

A NapC/NirT‐type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes

Microbial nitrate respiration – Genes, enzymes and environmental distribution

The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774

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