메뉴 건너뛰기




Volumn 181, Issue 1, 1999, Pages 241-245

A membrane-bound NAD(P)+-reducing hydrogenase provides reduced pyridine nucleotides during citrate fermentation by Klebsiella pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

CITRIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE;

EID: 0032930779     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.1.241-245.1999     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0028568063 scopus 로고
    • Nickel hydrogenases: In search of the active site
    • Albracht, S. P. J. 1994. Nickel hydrogenases: in search of the active site. Biochim. Biophys. Acta 1188:167-204.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 167-204
    • Albracht, S.P.J.1
  • 2
    • 0016229937 scopus 로고
    • Osmotically induced volume and turbidity changes of Escherichia coli due to salts, sucrose and glycerol, with particular reference to the rapid permeation of glycerol into the cell
    • Alemohammad, M. M., and C. J. Knowles. 1974. Osmotically induced volume and turbidity changes of Escherichia coli due to salts, sucrose and glycerol, with particular reference to the rapid permeation of glycerol into the cell. J. Gen. Microbiol. 82:125-142.
    • (1974) J. Gen. Microbiol. , vol.82 , pp. 125-142
    • Alemohammad, M.M.1    Knowles, C.J.2
  • 3
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Andrews, S. C., B. C. Berks, J. McClay, A. Ambler, M. A. Quail, P. Golby, and J. R. Guest. 1997. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143:3613-3647.
    • (1997) Microbiology , vol.143 , pp. 3613-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 4
    • 0000190996 scopus 로고    scopus 로고
    • Fermentation
    • F. C. Neidhardt, R. Curtiss III. J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik. W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umharger (ed.). American Society for Microbiology, Washington, D.C.
    • Böck, A., and G. Sawers. 1996. Fermentation, p. 262-282. In F. C. Neidhardt, R. Curtiss III. J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik. W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umharger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 262-282
    • Böck, A.1    Sawers, G.2
  • 5
    • 0030893492 scopus 로고    scopus 로고
    • Anaerobic citrate metabolism and its regulation in enterobacteria
    • Bott, M. 1997. Anaerobic citrate metabolism and its regulation in enterobacteria. Arch. Microbiol. 167:78-88.
    • (1997) Arch. Microbiol. , vol.167 , pp. 78-88
    • Bott, M.1
  • 6
    • 0004070117 scopus 로고
    • The anaerobic dissimilation of citric acid by Aerobacter indologenes
    • Brewer, C. R., and C. H. Werkman. 1939. The anaerobic dissimilation of citric acid by Aerobacter indologenes. Enzymologia 6:273-281.
    • (1939) Enzymologia , vol.6 , pp. 273-281
    • Brewer, C.R.1    Werkman, C.H.2
  • 7
    • 0039390359 scopus 로고
    • Spectrophotometry of intracellular respiratory pigments
    • Chance, B. 1954. Spectrophotometry of intracellular respiratory pigments. Science 120:767-775.
    • (1954) Science , vol.120 , pp. 767-775
    • Chance, B.1
  • 8
    • 0000602923 scopus 로고
    • Citric acid metabolism of Aerobacter aerogenes
    • Dagley, S., and E. A. Dawes. 1953. Citric acid metabolism of Aerobacter aerogenes. J. Bacteriol. 66:259-265.
    • (1953) J. Bacteriol. , vol.66 , pp. 259-265
    • Dagley, S.1    Dawes, E.A.2
  • 9
    • 0022558562 scopus 로고
    • Preparation, characterization, and reconstitution of oxaloacetate decarboxylase from Klebsiella aerogenes, a sodium pump
    • Dimroth, P. 1986. Preparation, characterization, and reconstitution of oxaloacetate decarboxylase from Klebsiella aerogenes, a sodium pump. Methods Enzymol. 125:530-540.
    • (1986) Methods Enzymol. , vol.125 , pp. 530-540
    • Dimroth, P.1
  • 10
    • 85064695528 scopus 로고
    • The role of vitamins and their carrier proteins in citrate fermentation
    • H. Kleinkauf, H. Von Döhren. and J. Jaenicke (ed.). De Gruyter, Berlin, Germany.
    • Dimroth, P. 1988. The role of vitamins and their carrier proteins in citrate fermentation, p. 191-204. In H. Kleinkauf, H. Von Döhren. and J. Jaenicke (ed.), The roots of modern biochemistry. De Gruyter, Berlin, Germany.
    • (1988) The Roots of Modern Biochemistry , pp. 191-204
    • Dimroth, P.1
  • 11
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • Dimroth, P. 1997. Primary sodium ion translocating enzymes. Biochim. Biophys. Acta 1318:11-51.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 12
    • 0024526420 scopus 로고
    • + -dependent NADH:Quinone oxidoreductase of Klebsiella pneumoniae
    • + -dependent NADH:quinone oxidoreductase of Klebsiella pneumoniae. Arch. Microbiol. 151:439-444.
    • (1989) Arch. Microbiol. , vol.151 , pp. 439-444
    • Dimroth, P.1    Thomer, A.2
  • 13
    • 0019419819 scopus 로고
    • Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus
    • Friedrich, B., E. Heine, A. Finck, and C. G. Friedrich. 1981. Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus. J. Bacteriol. 145:1144-1149.
    • (1981) J. Bacteriol. , vol.145 , pp. 1144-1149
    • Friedrich, B.1    Heine, E.2    Finck, A.3    Friedrich, C.G.4
  • 14
    • 0027382485 scopus 로고
    • Molecular biology of hydrogen utilization in aerobic chemolithotrophs
    • Friedrich, B., and E. Schwartz. 1993. Molecular biology of hydrogen utilization in aerobic chemolithotrophs. Annu. Rev. Microbiol. 47:351-383.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 351-383
    • Friedrich, B.1    Schwartz, E.2
  • 15
    • 33847087457 scopus 로고
    • Citrate conformation and chelation: Enzymatic implications
    • Glusker, J. P. 1980. Citrate conformation and chelation: enzymatic implications. Acc. Chcm. Res. 13:345-352.
    • (1980) Acc. Chcm. Res. , vol.13 , pp. 345-352
    • Glusker, J.P.1
  • 16
    • 0029803262 scopus 로고    scopus 로고
    • Sodium-ion dependent hydrogen production in Acidaminococcus fermentons
    • Härtel, U., and W. Buckel. 1996. Sodium-ion dependent hydrogen production in Acidaminococcus fermentons. Arch. Microbiol. 166:350-356.
    • (1996) Arch. Microbiol. , vol.166 , pp. 350-356
    • Härtel, U.1    Buckel, W.2
  • 17
    • 0029839587 scopus 로고    scopus 로고
    • Fermentation of trans-aconitate via citrate, oxaloacetate, and pyruvate by Acidaminococcus fermentaus
    • Härtel, U., and W. Buckel. 1996. Fermentation of trans-aconitate via citrate, oxaloacetate, and pyruvate by Acidaminococcus fermentaus. Arch. Microbiol. 166:342-349.
    • (1996) Arch. Microbiol. , vol.166 , pp. 342-349
    • Härtel, U.1    Buckel, W.2
  • 18
    • 0028966952 scopus 로고
    • Kinetic studies of the soluble hydrogenase from Alcaligenes eutrophus H16
    • Keefe, R. G., M. J. Axley, and A. L. Harabin. 1995. Kinetic studies of the soluble hydrogenase from Alcaligenes eutrophus H16. Arch. Biochem. Biophys. 317:449-456.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 449-456
    • Keefe, R.G.1    Axley, M.J.2    Harabin, A.L.3
  • 20
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • Malki, S., I. Saimmaime, G. de Luca, M. Rousset, Z. Dermoun and J.-P. Belaich. 1995. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bacteriol. 177:2628-2636.
    • (1995) J. Bacteriol. , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.-P.6
  • 21
    • 0014512439 scopus 로고
    • Requirement for sodium in the anaerobic growth of Aerobacter aerogenes on citrate
    • O'Brien, R. W., and J. R. Stern. 1969. Requirement for sodium in the anaerobic growth of Aerobacter aerogenes on citrate. J. Bacteriol. 98:388-393.
    • (1969) J. Bacteriol. , vol.98 , pp. 388-393
    • O'Brien, R.W.1    Stern, J.R.2
  • 22
    • 0018691912 scopus 로고
    • Evidence for two functionally distinct hydrogenases in anacystis nidulans
    • Peschek, G. A. 1979. Evidence for two functionally distinct hydrogenases in Anacystis nidulans. Arch. Microbiol. 123:81-92.
    • (1979) Arch. Microbiol. , vol.123 , pp. 81-92
    • Peschek, G.A.1
  • 23
    • 0026681774 scopus 로고
    • +-coupled reversed electron transfer in Klebsiella pneumoniae
    • +-coupled reversed electron transfer in Klebsiella pneumoniae. Mol. Microbiol. 6:1943-1948.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1943-1948
    • Pfenninger-Li, X.U.1    Dimroth, P.2
  • 24
    • 0030042331 scopus 로고    scopus 로고
    • + -dependent citrate carrier of Klebsiella pneumoniae: Evidence for asymmetric orientation of the carrier protein in proteoliposomes
    • + -dependent citrate carrier of Klebsiella pneumoniae: evidence for asymmetric orientation of the carrier protein in proteoliposomes. Biochemistry 35:1018-1026.
    • (1996) Biochemistry , vol.35 , pp. 1018-1026
    • Pos, K.M.1    Dimroth, P.2
  • 25
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of escherichia coli hydrogenase 3 requires nickel incorporation followed by c-terminal processing at Arg537
    • Rossmann. R., M. Sauter, F. Lottspeich, and A. Böck. 1994. Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537. Eur. J. Biochem. 20:377-384.
    • (1994) Eur. J. Biochem. , vol.20 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Böck, A.4
  • 27
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • Sawers, G. 1994. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Leeuwenhock 66:57-88.
    • (1994) Antonie Leeuwenhock , vol.66 , pp. 57-88
    • Sawers, G.1
  • 28
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymcs in Escherichia coli K-12: Evidence for a third isoenzyme
    • Sawers, R. G., S. P. Ballantine, and D. H. Boxer. 1985. Differential expression of hydrogenase isoenzymcs in Escherichia coli K-12: evidence for a third isoenzyme. J. Bacleriol. 164:1324-1331.
    • (1985) J. Bacleriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 29
    • 0028148806 scopus 로고
    • Energetics of syntrophic fatty acid oxidation
    • Schink, B., and M. Friedrich. 1994. Energetics of syntrophic fatty acid oxidation. FEMS Microbiol. Rev. 15:85-94.
    • (1994) FEMS Microbiol. Rev. , vol.15 , pp. 85-94
    • Schink, B.1    Friedrich, M.2
  • 30
    • 0017110320 scopus 로고
    • Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16
    • Schneider, K., and H. G. Schlegel. 1976. Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16. Biochim. Biophys. Acta 452:66-80.
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 66-80
    • Schneider, K.1    Schlegel, H.G.2
  • 33
    • 0015365891 scopus 로고
    • Levels of nicotinamide dinucleotide and reduced nicotinamide dinucleotide in facultative bacteria and the effect of oxygen
    • Wimpenny, J. W., and A. Firth. 1972. Levels of nicotinamide dinucleotide and reduced nicotinamide dinucleotide in facultative bacteria and the effect of oxygen. J. Bacteriol. 111:24-32.
    • (1972) J. Bacteriol. , vol.111 , pp. 24-32
    • Wimpenny, J.W.1    Firth, A.2
  • 34
    • 0027167618 scopus 로고
    • Microbial hydrogenases: Primary structure, classification, signatures and phylogeny
    • Wu, L. F., and M. A. Mandrand. 1993. Microbial hydrogenases: primary structure, classification, signatures and phylogeny. FEMS Microbiol. Rev. 104:243-270.
    • (1993) FEMS Microbiol. Rev. , vol.104 , pp. 243-270
    • Wu, L.F.1    Mandrand, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.