메뉴 건너뛰기




Volumn 272, Issue 15, 2005, Pages 3899-3908

Enlarging the gas access channel to the active site renders the regulatory hydrogenase HupUV of Rhodobacter capsulatus O2 sensitive without affecting its transductory activity

Author keywords

Gas access channel; Hydrogenases; Oxygen sensitivity; Rhodobacter capsulatus

Indexed keywords

BACTERIAL PROTEIN; HYDROGENASE; ISOLEUCINE; LEUCINE; PARAQUAT; PHENYLALANINE; PROTEIN HUPUV; UNCLASSIFIED DRUG; VALINE;

EID: 23644448705     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04806.x     Document Type: Article
Times cited : (73)

References (49)
  • 1
  • 2
    • 2142653130 scopus 로고    scopus 로고
    • Molecular biology of microbial hydrogenases
    • Vignais PM & Colbeau A (2004) Molecular biology of microbial hydrogenases. Curr Issues Mol Biol 6, 159-188.
    • (2004) Curr Issues Mol Biol , vol.6 , pp. 159-188
    • Vignais, P.M.1    Colbeau, A.2
  • 3
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams MW (1990) The structure and mechanism of iron-hydrogenases. Biochim Biophys Acta 1020, 115-145.
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 115-145
    • Adams, M.W.1
  • 4
    • 0003723366 scopus 로고    scopus 로고
    • Spectroscopy - The functional puzzle
    • (Cammack R, Frey M & Robson R, eds). Taylor & Francis, London
    • Albracht SPJ (2001) Spectroscopy-the functional puzzle. In Hydrogen as a Fuel. Learning from Nature (Cammack R, Frey M & Robson R, eds), pp. 110-158. Taylor & Francis, London.
    • (2001) Hydrogen As a Fuel. Learning from Nature , pp. 110-158
    • Albracht, S.P.J.1
  • 5
    • 1642305975 scopus 로고    scopus 로고
    • The catalytic machinery
    • (Cammack, R, Frey M & Robson R, eds). Taylor & Francis, London
    • Cammack R (2001) The catalytic machinery. In Hydrogen as a Fuel. Learning from Nature (Cammack, R, Frey M & Robson R, eds), pp. 159-180. Taylor & Francis, London.
    • (2001) Hydrogen As a Fuel. Learning from Nature , pp. 159-180
    • Cammack, R.1
  • 7
    • 0035175063 scopus 로고    scopus 로고
    • The [Ni-Fe] hydrogenase from Allochromatium vinosum was studied in EPR-detectable states: H/D exchange experiments that yield new information about the structure of the active site
    • Bleijlevens B, Faber BW & Albracht SPJ (2001) The [Ni-Fe] hydrogenase from Allochromatium vinosum was studied in EPR-detectable states: H/D exchange experiments that yield new information about the structure of the active site. J Biol Inorg Chem 6, 763-769.
    • (2001) J Biol Inorg Chem , vol.6 , pp. 763-769
    • Bleijlevens, B.1    Faber, B.W.2    Albracht, S.P.J.3
  • 12
    • 0029812909 scopus 로고    scopus 로고
    • The hupTUV operon is involved in negative control of hydrogenase synthesis in Rhodobacter capsulatus
    • Elsen S, Colbeau A, Chabert J & Vignais PM (1996) The hupTUV operon is involved in negative control of hydrogenase synthesis in Rhodobacter capsulatus. J Bacteriol 178, 5174-5181.
    • (1996) J Bacteriol , vol.178 , pp. 5174-5181
    • Elsen, S.1    Colbeau, A.2    Chabert, J.3    Vignais, P.M.4
  • 13
    • 0344666703 scopus 로고    scopus 로고
    • 2 sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus
    • 2 sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus. J Bacteriol 185, 7111-7119.
    • (2003) J Bacteriol , vol.185 , pp. 7111-7119
    • Elsen, S.1    Duché, O.2    Colbeau, A.3
  • 15
    • 0028007441 scopus 로고
    • Sequences and characterization of hupU and hupV genes of Bradyrhizobium japonicum encoding a possible nickel-sensing complex involved in hydrogenase expression
    • Black LK, Fu C & Maier RJ (1994) Sequences and characterization of hupU and hupV genes of Bradyrhizobium japonicum encoding a possible nickel-sensing complex involved in hydrogenase expression. J Bacteriol 176, 7102-7106.
    • (1994) J Bacteriol , vol.176 , pp. 7102-7106
    • Black, L.K.1    Fu, C.2    Maier, R.J.3
  • 20
    • 0033456155 scopus 로고    scopus 로고
    • The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system
    • Dischert W, Vignais PM & Colbeau A (1999) The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system. Mol Microbiol 34, 995-1006.
    • (1999) Mol Microbiol , vol.34 , pp. 995-1006
    • Dischert, W.1    Vignais, P.M.2    Colbeau, A.3
  • 21
    • 1642442726 scopus 로고    scopus 로고
    • 2-sensing complex of Ralstonia eutropha: Interaction between a regulatory [NiFe]hydrogenase and a histidine protein kinase
    • 2-sensing complex of Ralstonia eutropha: interaction between a regulatory [NiFe]hydrogenase and a histidine protein kinase. Mol Microbiol 51, 1677-1689.
    • (2004) Mol Microbiol , vol.51 , pp. 1677-1689
    • Buhrke, T.1    Lenz, O.2    Porthun, A.3    Friedrich, B.4
  • 26
    • 0017342164 scopus 로고
    • Molecular weights of protein multimers from polyacrylamide gel electrophoresis
    • Bryan JK (1977) Molecular weights of protein multimers from polyacrylamide gel electrophoresis. Anal Biochem 78, 513-519.
    • (1977) Anal Biochem , vol.78 , pp. 513-519
    • Bryan, J.K.1
  • 27
    • 6344283517 scopus 로고    scopus 로고
    • Hydrogenases and their activities
    • (Cammack R, Frey M & Robson R, eds). Taylor & Francis, London
    • Cammack R (2001) Hydrogenases and their activities. In Hydrogen as a Fuel. Learning from Nature (Cammack R, Frey M & Robson R, eds), pp. 73-92. Taylor & Francis, London.
    • (2001) Hydrogen As a Fuel. Learning from Nature , pp. 73-92
    • Cammack, R.1
  • 28
    • 0025727991 scopus 로고
    • Expression of regulatory nif genes in Rhodobacter capsulatus
    • Hübner P, Willison JC, Vignais PM & Bickle TA (1991) Expression of regulatory nif genes in Rhodobacter capsulatus. J Bacteriol 173, 2993-2999.
    • (1991) J Bacteriol , vol.173 , pp. 2993-2999
    • Hübner, P.1    Willison, J.C.2    Vignais, P.M.3    Bickle, T.A.4
  • 29
    • 2542565159 scopus 로고    scopus 로고
    • Hydrogen-induced activation of the [NiFe]-hydrogenase from Allochromatium vinosum as studied by stopped-flow infrared spectroscopy
    • Kurkin S, George SJ, Thorneley RNF & Albracht SPJ (2004) Hydrogen-induced activation of the [NiFe]-hydrogenase from Allochromatium vinosum as studied by stopped-flow infrared spectroscopy. Biochemistry 43, 6820-6831.
    • (2004) Biochemistry , vol.43 , pp. 6820-6831
    • Kurkin, S.1    George, S.J.2    Thorneley, R.N.F.3    Albracht, S.P.J.4
  • 31
    • 0018795813 scopus 로고
    • The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus
    • Schneider K, Schlegel HJ, Cammack R & Hall DO (1979) The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus. Biochim Biophys Acta 578, 445-461.
    • (1979) Biochim Biophys Acta , vol.578 , pp. 445-461
    • Schneider, K.1    Schlegel, H.J.2    Cammack, R.3    Hall, D.O.4
  • 32
    • 3943058946 scopus 로고    scopus 로고
    • The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
    • Van der Linden E, Burgdorf T, Bernhard B, Bleijlevens B, Friedrich B & Albracht SPJ (2004) The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen. J Biol Inorg Chem 9, 616-626.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 616-626
    • Van Der Linden, E.1    Burgdorf, T.2    Bernhard, B.3    Bleijlevens, B.4    Friedrich, B.5    Albracht, S.P.J.6
  • 34
    • 0031785260 scopus 로고    scopus 로고
    • hoxX (hypX) is a functional member of the Alcaligenes eutrophus hyp gene cluster
    • Buhrke T & Friedrich B (1998) hoxX (hypX) is a functional member of the Alcaligenes eutrophus hyp gene cluster. Arch Microbiol 170, 460-463.
    • (1998) Arch Microbiol , vol.170 , pp. 460-463
    • Buhrke, T.1    Friedrich, B.2
  • 35
    • 8744311816 scopus 로고    scopus 로고
    • The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel
    • Bleijlevens B, Buhrke T, Van der Linden E, Friedrich B & Albracht SPJ (2004) The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel. J Biol Chem 279, 46686-46689.
    • (2004) J Biol Chem , vol.279 , pp. 46686-46689
    • Bleijlevens, B.1    Buhrke, T.2    Van Der Linden, E.3    Friedrich, B.4    Albracht, S.P.J.5
  • 36
    • 0029841365 scopus 로고    scopus 로고
    • The hydrogenase gene cluster of Rhizobium leguminosarum bv viciae contains an additional gene (hypX) which encodes a protein with sequence similarity to the N10-formyltetra-hydrofolate-dependent enzyme family and is required for nickel-dependent hydrogenase processing and activity
    • Rey L, Fernandez D, Brito B, Hernando Y, Palacios JM, Imperial J & Ruiz-Argueso T (1996) The hydrogenase gene cluster of Rhizobium leguminosarum bv viciae contains an additional gene (hypX) which encodes a protein with sequence similarity to the N10-formyltetra-hydrofolate-dependent enzyme family and is required for nickel-dependent hydrogenase processing and activity. Mol General Genet 252, 237-248.
    • (1996) Mol General Genet , vol.252 , pp. 237-248
    • Rey, L.1    Fernandez, D.2    Brito, B.3    Hernando, Y.4    Palacios, J.M.5    Imperial, J.6    Ruiz-Argueso, T.7
  • 38
    • 0142152415 scopus 로고    scopus 로고
    • 2-sensing hydrogenase from Ralstonia eutropha in its reduced state by HYSCORE and ENDOR spectroscopy
    • 2-sensing hydrogenase from Ralstonia eutropha in its reduced state by HYSCORE and ENDOR spectroscopy. J Am Chem Soc 125, 13075-13083.
    • (2003) J Am Chem Soc , vol.125 , pp. 13075-13083
    • Brecht, M.1    Van Gastel, M.2    Burhke, T.3    Friedrich, B.4    Lubitz, W.5
  • 39
    • 0141542719 scopus 로고    scopus 로고
    • Hydrogen-induced structural changes at the nickel site of the regulatory [NiFe]hydrogenase from Ralstonia eutropha detected by X-ray absorption spectroscopy
    • Haumann M, Porthun A, Buhrke T, Liebisch P, Meyer-Klaucke W, Friedrich B & Dau H (2003) Hydrogen-induced structural changes at the nickel site of the regulatory [NiFe]hydrogenase from Ralstonia eutropha detected by X-ray absorption spectroscopy. Biochemistry 42, 11004-11015.
    • (2003) Biochemistry , vol.42 , pp. 11004-11015
    • Haumann, M.1    Porthun, A.2    Buhrke, T.3    Liebisch, P.4    Meyer-Klaucke, W.5    Friedrich, B.6    Dau, H.7
  • 40
    • 21244441201 scopus 로고    scopus 로고
    • 2-sensing [NiFe] hydrogenase from Ralstoniae utropho H16 is based on limited access of oxygen to the active site
    • in press
    • 2-sensing [NiFe] hydrogenase from Ralstoniae utropho H16 is based on limited access of oxygen to the active site. J Biol Chem in press.
    • (2005) J Biol Chem
    • Buhrke, T.1    Lenz, O.2    Krauss, N.3    Friedrich, B.4
  • 42
    • 0022634952 scopus 로고
    • Cloning of DNA fragments carrying hydrogenase genes of Rhodopseudomonas capsulata
    • Colbeau A, Godfroy A & Vignais PM (1986) Cloning of DNA fragments carrying hydrogenase genes of Rhodopseudomonas capsulata. Biochimie 68, 147-155.
    • (1986) Biochimie , vol.68 , pp. 147-155
    • Colbeau, A.1    Godfroy, A.2    Vignais, P.M.3
  • 43
    • 0019157954 scopus 로고
    • Hydrogenase activity in Rhodopseudomonas capsulata: Relationship with nitrogenase activity
    • Colbeau A, Kelley BC & Vignais PM (1980) Hydrogenase activity in Rhodopseudomonas capsulata: relationship with nitrogenase activity. J Bacteriol 144, 141-148.
    • (1980) J Bacteriol , vol.144 , pp. 141-148
    • Colbeau, A.1    Kelley, B.C.2    Vignais, P.M.3
  • 44
    • 1542286924 scopus 로고    scopus 로고
    • Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp. strain PCC 6803 deficient in the type I NADPH-dehydrogenase complex
    • Cournac L, Guedeney G, Peltier G & Vignais PM (2004) Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp. strain PCC 6803 deficient in the type I NADPH-dehydrogenase complex. J Bacteriol 186, 1737-1746.
    • (2004) J Bacteriol , vol.186 , pp. 1737-1746
    • Cournac, L.1    Guedeney, G.2    Peltier, G.3    Vignais, P.M.4
  • 45
    • 0016381336 scopus 로고
    • Genetic recombination in Rhodopseudomonas capsulata
    • Marrs B (1974) Genetic recombination in Rhodopseudomonas capsulata. Proc Natl Acad Sci USA 71, 971-973.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 971-973
    • Marrs, B.1
  • 46
    • 0025136740 scopus 로고
    • Genetic and physical mapping of an hydrogenase gene cluster from Rhodobacter capsulatus
    • Colbeau A, Magnin JP, Cauvin B, Champion T & Vignais PM (1990) Genetic and physical mapping of an hydrogenase gene cluster from Rhodobacter capsulatus. Mol General Genet 220, 393-399.
    • (1990) Mol General Genet , vol.220 , pp. 393-399
    • Colbeau, A.1    Magnin, J.P.2    Cauvin, B.3    Champion, T.4    Vignais, P.M.5
  • 47
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C, Vieira J & Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 48
    • 0028225567 scopus 로고
    • A new gene expression system based on a fructose-dependent promoter from Rhodobacter capsulatus
    • Duport C, Meyer C, Naud I & Jouanneau Y (1994) A new gene expression system based on a fructose-dependent promoter from Rhodobacter capsulatus. Gene 145, 103-108.
    • (1994) Gene , vol.145 , pp. 103-108
    • Duport, C.1    Meyer, C.2    Naud, I.3    Jouanneau, Y.4
  • 49
    • 1842349188 scopus 로고
    • Broad-host range DNA cloning system for gram-negative bacteria: Construction of a gene bank of Rhizobium meliloti
    • Ditta G, Stanfield S, Corbin D & Helinski DP (1980) Broad-host range DNA cloning system for gram-negative bacteria: construction of a gene bank of Rhizobium meliloti. Proc Natl Acad Sci USA 77, 7347-7351.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7347-7351
    • Ditta, G.1    Stanfield, S.2    Corbin, D.3    Helinski, D.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.