Cloning and sequences of the structural (hupSLC) and accessory (hupDHI) genes for hydrogenase biosynthesis in Thiocapsa roseopersicina
References (36)
- et al.
Two open reading frames (ORFs) identified near the hydrogenase structural genes in Azotobacter vinelandii, the first ORF may encode for a polypeptide similar to rubredoxins
Biochim. Biophys. Acta
(1992) - et al.
The properties of hydrogenase from Thiocapsa roseopersicina
Biochim. Biophys. Acta
(1978) - et al.
A small cosmid for efficient cloning of large DNA fragments
Gene
(1980) - et al.
Structural rearrangements in active and inactive forms of hydrogenase from Thiocapsa roseopersicina
J. Biol. Chem.
(1991) - et al.
Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase1
J. Bacteriol.
(1991) - et al.
Molecular biology studies of the uptake hydrogenase of Rhodobacter capsulatus and Rhodocyclus gelatinosus
FEMS Microbiol. Rev. vn87
(1990) - et al.
A mutation in Rhodobacter capsulatus gene encoding an integration host factor-like protein impairs in vivo hydrogenase expression
- et al.
Molecular biology of membranebound H2 uptake hydrogenases
Arch. Microbiol.
(1994) - et al.
Characterization of Rhodopseudomonas capsulata
Arch. Microbiol.
(1975) - et al.
A rapid alkaline extraction procedure for screening recombinant plasmid DNA
Nucleic Acids Res.
(1979)
The hydrogenase structural operon in Rhodobacter cupsulatus contains a third gene, hupM, necessary for the formation of a physiologically competent hydrogenase
Mol. Microbiol.
Organisation of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two regulatory mutants
Mol. Microbiol.
The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes
Eur. J. Biochem.
Nucleotide sequence of the hydrogenase structural genes from Rhizobium leguminosarum
Plant Mol. Biol.
Nucleotide sequence and characterization of four additional genes of the hydrogenase structural operon from Rhizobium leguminosarum bv. viciae
J. Bacteriol.
A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16
J. Bacteriol.
Immunological relationships among hydrogenases
J. Bacteriol.
Cloning an sequencing of the genes encoding the large and the small subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus
Mol. Gen. Genet.
Cloning an sequencing of the genes encoding the large and the small subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus
Erratum
Cited by (40)
The HydS C-terminal domain of the Thiocapsa bogorovii HydSL hydrogenase is involved in membrane anchoring and electron transfer
2021, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :The purple sulfur bacterium Thiocapsa bogorovii BBS (previously named Thiocapsa roseopersicina) [ [2]; https://lpsn.dsmz.de/species/thiocapsa-bogorovii] contains at least five sets of structural genes and synthesizes at least four different hydrogenases, which have been shown to be regulated independently [3,4]. Genes of HupSLC hydrogenase were first discovered in T. bogorovii BBS [5]. This hydrogenase belongs to 1d subgroup.
Heterologous functionality and roles of conserved cysteine motifs of the [NiFe]-hydrogenase accessory protein, HupK/HoxV
2014, International Journal of Hydrogen EnergyCitation Excerpt :Nevertheless, variations in the general scheme can be anticipated, because T. roseopersicina expresses four hydrogenases associated with distinct metabolic functions [22]. In T. roseopersicina, few accessory genes were identified in the hydrogenase structural genes clusters (hupDHI, hoxW, hynH) [30,31], others (hypA, hypB, hypC1, hypC2, hypD, hypE, hypF, hynD and hupK) were scattered in the genome in several loci [26,27]. Analysis of ΔhupK mutant strains disclosed that HupK protein was important for the formation of the functionally active membrane-bound hydrogenases (HynSL and HupSL), but not for the biosynthesis of the soluble enzymes (Hox1, Hox2) [27].
Relationship between PHA and hydrogen metabolism in the purple sulfur phototrophic bacterium Thiocapsa roseopersicina BBS
2012, International Journal of Hydrogen EnergyCitation Excerpt :Our model organism, Thiocapsa roseopersicina BBS is a photosynthetic purple sulfur bacterium (PSB) which can be propagated photochemolitoautotrophically on reduced sulfur compounds and simple organic substrates such as acetate, succinate, pyruvate, glucose, etc. It contains four active [NiFe] hydrogenases: two of them are membrane-associated (HupSL, HynSL) [18,19], and Hox1 [20] and the recently described Hox2 [21] are soluble hydrogenases. This microbe is able to fix molecular nitrogen in the absence of alternative nitrogen sources.
Specificity and selectivity of HypC chaperonins and endopeptidases in the molecular assembly machinery of [NiFe] hydrogenases of Thiocapsa roseopersicina
2010, International Journal of Hydrogen EnergyCitation Excerpt :The phototrophic purple sulfur bacterium, Thiocapsa roseopersicina BBS can grow under various environmental conditions, it is cultivated usually phototrophically under anaerobic conditions in laboratory. The wild-type strain (BBS) harbours at least three functional [NiFe] hydrogenases (HupSL, HynSL, HoxEFUYH) [20–23] and a silent regulatory hydrogenase (HupTUV) [24]. The basic principles of [NiFe] hydrogenase maturation are expected to be valid for the hydrogenases of T. roseopersicina, as these ancient enzymes are well-conserved.
A novel approach for biohydrogen production
2006, International Journal of Hydrogen EnergyNovel approaches to exploit microbial hydrogen metabolism
2004, Biohydrogen III: Renewable Energy System by Biological Solar Energy Conversion
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