1993
DOI: 10.1007/bf00279903
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Identification of a new class of nitrogen fixation genes in Rhodobacter capsalatus: a putative membrane complex involved in electron transport to nitrogenase

Abstract: DNA sequence analysis of a 12236 bp fragment, which is located upstream of nifE in Rhodobacter capsulatus nif region A, revealed the presence of ten open reading frames. With the exception of fdxC and fdxN, which encode a plant-type and a bacterial-type ferredoxin, the deduced products of these coding regions exhibited no significant homology to known proteins. Analysis of defined insertion and deletion mutants demonstrated that six of these genes were required for nitrogen fixation. Therefore, we propose to c… Show more

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Cited by 252 publications
(255 citation statements)
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“…Furthermore, the genes for a membrane-bound electron transport chain could be identified in the genomes of C. tetani and C. perfringens. This system shows strong similarity to the Rhodobacter-specific nitrogen fixation system of Rhodobacter capsulatus as well as to the system NADH:ubiquinone oxidoreductase found in many aerobic pathogens such as V. cholerae, Salmonella typhimurium, Y. pestis, and Haemophilus influenzae, in which it apparently functions as a Na ϩ -translocating NADH dehydrogenase (32,36). Because there are no reports for quinones in clostridia, such a NADH dehydrogenase could be involved in the fermentation of amino acids by C. tetani, as indicated in Fig.…”
Section: Resultsmentioning
confidence: 73%
“…Furthermore, the genes for a membrane-bound electron transport chain could be identified in the genomes of C. tetani and C. perfringens. This system shows strong similarity to the Rhodobacter-specific nitrogen fixation system of Rhodobacter capsulatus as well as to the system NADH:ubiquinone oxidoreductase found in many aerobic pathogens such as V. cholerae, Salmonella typhimurium, Y. pestis, and Haemophilus influenzae, in which it apparently functions as a Na ϩ -translocating NADH dehydrogenase (32,36). Because there are no reports for quinones in clostridia, such a NADH dehydrogenase could be involved in the fermentation of amino acids by C. tetani, as indicated in Fig.…”
Section: Resultsmentioning
confidence: 73%
“…Reaction 5 principally resembles the coenzyme Q cycle in that twice the amount of electrons required for substrate reduction is fed into the cycle in which the flow of electrons is divided to react both with a high potential acceptor (crotonyl-CoA) and a low potential acceptor (ferredoxin). The reduced ferredoxin generated in reaction 5 is then used to regenerate NADH in reaction 6 catalyzed via a membrane-associated, energy-converting NADH: ferredoxin oxidoreductase (RnfA-G) (34,35 It is the combination of these reactions that allows explaining H 2 production by C. kluyveri and the generation of a proton motive force. The Bcd/EtfAB complex from C. kluyveri has been purified from the soluble cell fraction and was shown to catalyze reaction 5 (36).…”
Section: Ethanol Dehydrogenases and Acetaldehyde Dehydrogenases In Amentioning
confidence: 99%
“…Structural characterization of R. capsulatus FprA. R. capsu-(A) SDS/PAGE analysis : lane 1, molecular mass markers; lane 2, purilatus FprA was purified from E. coli JW195 overexpressing its fied FprA; lane 3, cross-linked FprA (with the position of the dimer structural gene, fprA, previously called ORF14 [9]. The purified shown by an arrow).…”
Section: % Between E Coli Orf479 and M Thermoautotrophicum Fectlymentioning
confidence: 99%
“…later. R. capsulatus fprA gene [9] was cloned and expressed in Spectra were recorded on a Cary 1E spectrophotometer run-E. coli strain JW195 according to procedures to be described ning the version 3.0 DOS software (Varian Associates) and on elsewhere (Jouanneau, Y., Meyer, C. and Willison, J., unpuba model HP8452 A apparatus (Hewlett-Packard). Data were then lished results).…”
mentioning
confidence: 99%