Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.12.7.2 (hydrogenase)
 3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hydrogenase gene from Clostridium butyricum was cloned in Escherichia coli HK16 (Hyd-) using pBR322 and PstI. The plasmid, pCBH1, containing hydrogenase gene was 7.3 MDa and pCBH1 had 5 PstI-DNA fragments (3.9, 2.6, 0.7, 0.03-0.04, less than 0.02 MDa, respectively). The hydrogenase activity of HK16 (pCBH1) was about 3.1-3.5-times as high as those of the present strains, such as C.butyricum and E.coli C600 (Hyd+).
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PMID:Cloning and expression of the hydrogenase gene from Clostridium butyricum in Escherichia coli. 634

It is shown that -2H+/K(+)-exchange through the H(+)-K(+)-pump, formed by the F0F1-ATPase and the Trk H system, H(+)-K(+)-exchange via H(+)-K(+)-antiporter, formed by the F0 and the Trk G (core) system [1-2], and production of H2 in anaerobically grown E.coli are changed in the mutants with defects in components of formate hydrogen lyase complex, oxidizing formate to CO2 and H2. 2H+/K(+)-exchange and H2 production are destroyed, but H(+)-K(+)-exchange with a variable stoichiometry for N,N'-dicyclohexyl-carbodiimide-sensitive ion fluxes is displayed in the fdhF mutant E.coli FM911, where formate dehydrogenase(H) is absent. 2H+/K(+)-exchange does not occur, but H(+)-K(+)-exchange with variable stoichiometry for N,N'-dicyclohexylcarbodiimide-sensitive ion fluxes and H2 production are observed in the uncD mutant E.coli AN817 with defect in beta subunit of the F1. Deletion of the hyc-operon in mutant E.coli HD700, led to absence of hydrogenase 3, destroys H(+)-K(+)-exchange and H2 production. H2 evaluation is shown in the E.coli K12(lambda) protoplasts, treated with toluene, by adding of NADH into the medium, containing ATP and K+. It is inhibited by N,N'-dicyclohexylcarbodiimide. H2 production is increased by adding of dithiothreitol, when NADH is changed by formate. It is lost in the mutants with defects in the F0 (E.coli AN936) or in the Trk A protein (E.coli TK2242). Dehydrogenase(H) and hydrogenase 3 are assumed to link mutually with a H(+)-K(+)-pump operation, reducing equivalents, necessary for a dithiol-disulfide interconversion within a mechanism of pump, are transferred from formate by means of dehydrogenase(H) to hydrogenase 3 through the F0F1 and the Trk H system to produce H2. It is assumed that hydrogenase 3 can interact with a mechanism of H(+)-K(+)-antiporter, NADH could serve as a donor of reducing equivalents. A role of thiol-groups and dithiol-disulfide interconversion in a functions of both mechanism for H(+)-K(+)-exchange is confirmed.
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PMID:[Role of components of formate-hydrogen-lyase in forming molecular hydrogen and their connection with proton-potassium exchange in anaerobically grown Escherichia coli]. 872 54