메뉴 건너뛰기




Volumn 33, Issue 4, 1998, Pages 590-600

Kinetics and interaction studies between cytochrome C3 and Fe-only hydrogenase from Desulfovibrio vulgaris Hildenborough

Author keywords

Fe hydrogenase; BIAcore analysis; Cooperativity; Crystallization; Protein protein interaction

Indexed keywords

CYTOCHROME C3; HYDROGENASE;

EID: 0032374034     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981201)33:4<590::AID-PROT11>3.0.CO;2-I     Document Type: Article
Times cited : (37)

References (65)
  • 1
    • 0021197001 scopus 로고
    • Hydrogenase, electron-transfer proteins, and energy coupling in the sulphate-reducing bacteria Desulfovibrio
    • Odom, J.M., Peck, H.D. Hydrogenase, electron-transfer proteins, and energy coupling in the sulphate-reducing bacteria Desulfovibrio. Annu. Rev. Microbiol. 38:551-592, 1984.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 551-592
    • Odom, J.M.1    Peck, H.D.2
  • 2
    • 0019802315 scopus 로고
    • Hydrogen cycling as a general mechanism for energy coupling in the sulfate-reducing bacterium, Desulfovibrio sp.
    • Odom, J., Peck, H.D. Jr. Hydrogen cycling as a general mechanism for energy coupling in the sulfate-reducing bacterium, Desulfovibrio sp. FEMS Microbiol. Lett. 12:47-50, 1981.
    • (1981) FEMS Microbiol. Lett. , vol.12 , pp. 47-50
    • Odom, J.1    Peck Jr., H.D.2
  • 3
    • 0021180562 scopus 로고
    • Physiological function of hydrogen metabolism during growth of sulfidogenic bacteria on organic substrates
    • Lupton, F.S., Conrad, R., Zeikus, J.G. Physiological function of hydrogen metabolism during growth of sulfidogenic bacteria on organic substrates. J. Bacteriol. 159:843-849, 1984.
    • (1984) J. Bacteriol. , vol.159 , pp. 843-849
    • Lupton, F.S.1    Conrad, R.2    Zeikus, J.G.3
  • 4
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams, M.W.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020:115-145, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 6
    • 0028672276 scopus 로고
    • Nickel-iron-selenium hydrogenase
    • Patil, D.S. Nickel-iron-selenium hydrogenase. Methods Enzymol. 243:68-94, 1994.
    • (1994) Methods Enzymol. , vol.243 , pp. 68-94
    • Patil, D.S.1
  • 7
    • 0021804386 scopus 로고
    • Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough)
    • Voordouw, G., Brenner, S. Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 148:515-520, 1985.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 515-520
    • Voordouw, G.1    Brenner, S.2
  • 8
    • 0023508107 scopus 로고
    • Cloning, characterization, and sequencing of the genes encoding the large and the small subunits of the periplasmic [NiFe] hydrogenase of Desulfovibrio gigas
    • Li, C., Peck, H.D. Jr., Przybyla, A.E. Cloning, characterization, and sequencing of the genes encoding the large and the small subunits of the periplasmic [NiFe] hydrogenase of Desulfovibrio gigas. DNA 6:539-551, 1987.
    • (1987) DNA , vol.6 , pp. 539-551
    • Li, C.1    Peck Jr., H.D.2    Przybyla, A.E.3
  • 9
    • 0023477185 scopus 로고
    • Cloning and sequencing of the genes encoding the large and small subunits of the periplasmic [NiFeSe] hydrogenase of Desulfovibrio baculatus
    • Menon, N.K., Peck, H.D. Jr, LeGall, J., Przybyla, A.E. Cloning and sequencing of the genes encoding the large and small subunits of the periplasmic [NiFeSe] hydrogenase of Desulfovibrio baculatus. J. Bacteriol. 169:5401-5407, 1987.
    • (1987) J. Bacteriol. , vol.169 , pp. 5401-5407
    • Menon, N.K.1    Peck Jr., H.D.2    LeGall, J.3    Przybyla, A.E.4
  • 12
    • 0024145465 scopus 로고
    • The three classes of hydrogenases from sulphate reducing bacteria of the genus Desulfovibrio
    • Fauque, G., Peck, H.D., Moura, J.J., et al. The three classes of hydrogenases from sulphate reducing bacteria of the genus Desulfovibrio. FEMS Microbiol. Rev. 4:299-344, 1988.
    • (1988) FEMS Microbiol. Rev. , vol.4 , pp. 299-344
    • Fauque, G.1    Peck, H.D.2    Moura, J.J.3
  • 13
    • 0023655356 scopus 로고
    • Inhibition studies of three classes of Desulfovibrio hydrogenase: Application to the further characterization of the multiple hydrogenases found in Desulfovibrio vulgaris Hildenborough
    • Berlier, Y., Fauque, G.D., LeGall, J., Choi, E.S., Peck, H.D. Jr., Lespinat, P.A. Inhibition studies of three classes of Desulfovibrio hydrogenase: application to the further characterization of the multiple hydrogenases found in Desulfovibrio vulgaris Hildenborough. Biochem. Biophys. Res. Commun. 146:147-153, 1987.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 147-153
    • Berlier, Y.1    Fauque, G.D.2    LeGall, J.3    Choi, E.S.4    Peck Jr., H.D.5    Lespinat, P.A.6
  • 14
    • 0025294858 scopus 로고
    • Localization of membrane-associated (NiFe) and (NiFeSe) hydrogenases of Desulfovibrio vulgaris using immunoelectron microscopic procedures
    • Rhode, M., Fürstenau, U., Mayer, F., et al. Localization of membrane-associated (NiFe) and (NiFeSe) hydrogenases of Desulfovibrio vulgaris using immunoelectron microscopic procedures. Eur. J. Biochem. 191:389-396, 1990.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 389-396
    • Rhode, M.1    Fürstenau, U.2    Mayer, F.3
  • 15
    • 0017812528 scopus 로고
    • Separation of hydrogenase from intact cells of Desulfovibrio vulgaris. Purification and properties
    • Van der Western, H.M., Mayhew, S.G., Veeger, C. Separation of hydrogenase from intact cells of Desulfovibrio vulgaris. Purification and properties. FEBS Lett. 86:122-126, 1978.
    • (1978) FEBS Lett. , vol.86 , pp. 122-126
    • Van Der Western, H.M.1    Mayhew, S.G.2    Veeger, C.3
  • 16
    • 0021880814 scopus 로고
    • Cloning of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough) and determination of the NH2-terminal sequence
    • Voordouw, G., Walker, J.E., Brenner, S. Cloning of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough) and determination of the NH2-terminal sequence. Eur. J. Biochem. 148:509-514, 1985.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 509-514
    • Voordouw, G.1    Walker, J.E.2    Brenner, S.3
  • 17
    • 0022451482 scopus 로고
    • Putative signal peptide on the small subunit of the periplasmic hydrogenase from Desulfovibrio vulgaris
    • Pickril, B.C., Czechowski, M.H., Przybyla, A.E., Peck, H.D., Le Gall, J. Putative signal peptide on the small subunit of the periplasmic hydrogenase from Desulfovibrio vulgaris. J. Bacteriol. 167:722-725, 1986.
    • (1986) J. Bacteriol. , vol.167 , pp. 722-725
    • Pickril, B.C.1    Czechowski, M.H.2    Przybyla, A.E.3    Peck, H.D.4    Le Gall, J.5
  • 18
    • 0022530699 scopus 로고
    • The iron-sulfur composition of the active site of hydrogenase from Desulfovibrio vulgaris (Hildenborough) deduced from its subunit structure and total iron-sulfur content
    • Hagen, W.R., van Berkel-Arts, A., Krüse-Wolters, K.M., Voordouw, G., Veeger, C. The iron-sulfur composition of the active site of hydrogenase from Desulfovibrio vulgaris (Hildenborough) deduced from its subunit structure and total iron-sulfur content. FEBS Lett. 203:59-63, 1986.
    • (1986) FEBS Lett. , vol.203 , pp. 59-63
    • Hagen, W.R.1    Van Berkel-Arts, A.2    Krüse-Wolters, K.M.3    Voordouw, G.4    Veeger, C.5
  • 19
    • 0029891513 scopus 로고    scopus 로고
    • Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrated spectroscopy
    • Van der Spek, T.M., Arendsen, A.F., Happe, R.P., et al. Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrated spectroscopy. Eur. J. Biochem. 237:629-634, 1996.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 629-634
    • Van Der Spek, T.M.1    Arendsen, A.F.2    Happe, R.P.3
  • 20
    • 0016122218 scopus 로고
    • Evidence for the periplasmic location of hydrogenase in Desulfovibrio gigas
    • Bell, H.G.R., LeGall, J., Peck, H.D. Jr. Evidence for the periplasmic location of hydrogenase in Desulfovibrio gigas. J. Bacteriol. 120:994-997, 1974.
    • (1974) J. Bacteriol. , vol.120 , pp. 994-997
    • Bell, H.G.R.1    LeGall, J.2    Peck Jr., H.D.3
  • 22
    • 0028671818 scopus 로고
    • 3 (Mr26000) isolated from sulfate-reducing bacteria and its relationships to other polyhemic cytochromes from Desulfovibrio
    • 3 (Mr26000) isolated from sulfate-reducing bacteria and its relationships to other polyhemic cytochromes from Desulfovibrio. Methods Enzymol. 243: 140-155, 1994.
    • (1994) Methods Enzymol. , vol.243 , pp. 140-155
    • Bruschi, M.1
  • 23
    • 0026084295 scopus 로고
    • Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough
    • Pollock, W.B.R., Loutfi, M., Bruschi, M., Rapp-Giles, B.J., Wall, J.D., Voordouw, G. Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 173: 220-228, 1991.
    • (1991) J. Bacteriol. , vol.173 , pp. 220-228
    • Pollock, W.B.R.1    Loutfi, M.2    Bruschi, M.3    Rapp-Giles, B.J.4    Wall, J.D.5    Voordouw, G.6
  • 24
    • 0002172471 scopus 로고
    • The structure and classification of cytochromes c
    • Robinson, A.B., Kaplan, N.O. (eds.). London: Academic Press
    • Ambler, R.P. The structure and classification of cytochromes c. In: "From Cyclotrons to Cytochromes." Robinson, A.B., Kaplan, N.O. (eds.). London: Academic Press 263-279, 1980.
    • (1980) From Cyclotrons to Cytochromes , pp. 263-279
    • Ambler, R.P.1
  • 28
    • 0021902977 scopus 로고
    • The structure, function and evolution of cytochromes
    • Mathews, F.S. The structure, function and evolution of cytochromes. Prog. Biophys. Mol. Biol. 45:1-56, 1985.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 1-56
    • Mathews, F.S.1
  • 29
    • 0000647672 scopus 로고
    • Enzymatic conversion of apolar compounds in organic media using an NADH-regenerating system and dihydrogen as reductant
    • Hilhorst, R., Laane, C., Veeger, C. Enzymatic conversion of apolar compounds in organic media using an NADH-regenerating system and dihydrogen as reductant. FEBS Lett. 159, 225-228, 1983.
    • (1983) FEBS Lett. , vol.159 , pp. 225-228
    • Hilhorst, R.1    Laane, C.2    Veeger, C.3
  • 30
    • 0027372952 scopus 로고
    • Voltammetric studies of the catalytic electron-transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus
    • Moreno, C., Franco, R., Moura, I., LeGall, J., Moura, J.G. Voltammetric studies of the catalytic electron-transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus. Eur. J. Biochem. 217:981-989, 1993.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 981-989
    • Moreno, C.1    Franco, R.2    Moura, I.3    LeGall, J.4    Moura, J.G.5
  • 34
    • 0004080075 scopus 로고
    • Cambridge: Cambridge University Press
    • nd edit. Cambridge: Cambridge University Press, 1984:24-41.
    • (1984) nd Edit. , pp. 24-41
    • Postgate, J.R.1
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0017170673 scopus 로고
    • 450 on sodium dodecyl sulfate polyacrylamide gels
    • 450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 75:168-176, 1976.
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 39
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J., Kim, S.H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411, 1991.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 40
    • 0022321627 scopus 로고
    • Crystallization of macromolecules: General principles
    • McPherson, A. Crystallization of macromolecules: general principles. Methods Enzymol. 114:112-120, 1989.
    • (1989) Methods Enzymol. , vol.114 , pp. 112-120
    • McPherson, A.1
  • 42
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 43
    • 0022632534 scopus 로고
    • 3 and ferredoxin from Desulfovibrio desulfuricans Norway strain and their individual reactions with dithionite
    • 3 and ferredoxin from Desulfovibrio desulfuricans Norway strain and their individual reactions with dithionite. Biochim. Biophys. Acta 848:279-293, 1986.
    • (1986) Biochim. Biophys. Acta , vol.848 , pp. 279-293
    • Capeillère-Blandin, C.1    Guerlesquin, F.2    Bruschi, M.3
  • 45
    • 0030478020 scopus 로고    scopus 로고
    • Kinetic analysis of biosensor data: Elementary tests for self-consistency
    • Schuck, P., and Minton, C. Kinetic analysis of biosensor data: elementary tests for self-consistency. Trends Biochem. Sci. 12:458-460, 1996.
    • (1996) Trends Biochem. Sci. , vol.12 , pp. 458-460
    • Schuck, P.1    Minton, C.2
  • 46
    • 5244365457 scopus 로고
    • The influence of metal ions on the activity of hydrogenase in sulphate reducing bacteria
    • Cheung, C.W.S., Beech, I.B. The influence of metal ions on the activity of hydrogenase in sulphate reducing bacteria. Eur. Fed. Corrosion Publications 15:169-180, 1995.
    • (1995) Eur. Fed. Corrosion Publications , vol.15 , pp. 169-180
    • Cheung, C.W.S.1    Beech, I.B.2
  • 47
    • 0027406970 scopus 로고
    • Regulation of the periplasmic [Fe] hydrogenase by ferrous iron in Desulfovibrio vulgaris (Hildenborough)
    • Bryant, R.D., Van Ommen Kloeke, F., Laishley, E.J. Regulation of the periplasmic [Fe] hydrogenase by ferrous iron in Desulfovibrio vulgaris (Hildenborough). Appl. Environ. Microbiol. 59:491-495, 1993.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 491-495
    • Bryant, R.D.1    Van Ommen Kloeke, F.2    Laishley, E.J.3
  • 48
    • 0030885964 scopus 로고    scopus 로고
    • Metals control activity and expression of the heme biosynthesis enzyme δ-aminolevulinic acid dehydratase in Bradyrhizobium japonicum
    • Chauhan, S., Douglas, E.T., O'Bryan, M.R. Metals control activity and expression of the heme biosynthesis enzyme δ-aminolevulinic acid dehydratase in Bradyrhizobium japonicum. J. Bacteriol. 179:5516-5520, 1997.
    • (1997) J. Bacteriol. , vol.179 , pp. 5516-5520
    • Chauhan, S.1    Douglas, E.T.2    O'Bryan, M.R.3
  • 49
    • 0030666834 scopus 로고    scopus 로고
    • Genetic diversity and expression of the [NiFe] hydrogenase large-subunit gene of Desulfovibrio spp. in environmental samples
    • Wawer, C., Jetten, M.S.M., Muyzer, G. Genetic diversity and expression of the [NiFe] hydrogenase large-subunit gene of Desulfovibrio spp. in environmental samples. Appl. Environ. Microbiol. 63:4360-4369, 1997.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4360-4369
    • Wawer, C.1    Jetten, M.S.M.2    Muyzer, G.3
  • 50
    • 0027161364 scopus 로고
    • The operon for the Fe-hydrogenase in Desulfovibrio vulgaris (Hildenborough): Mapping of the transcript and regulation of expression
    • Van den Berg, W.A.M., Stokkermans, J.P.W.G., Van Dongen, W.M.A.M. The operon for the Fe-hydrogenase in Desulfovibrio vulgaris (Hildenborough): mapping of the transcript and regulation of expression. FEMS Lett. 110:85-90, 1993.
    • (1993) FEMS Lett. , vol.110 , pp. 85-90
    • Van Den Berg, W.A.M.1    Stokkermans, J.P.W.G.2    Van Dongen, W.M.A.M.3
  • 52
    • 0024316849 scopus 로고
    • Electron transport in sulfate reducing bacteria
    • Stewart, I.M.V., Le Gall, J., Moura, I., et al. Electron transport in sulfate reducing bacteria. Eur. J. Biochem. 185:695-700, 1989.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 695-700
    • Stewart, I.M.V.1    Le Gall, J.2    Moura, I.3
  • 54
    • 0024286094 scopus 로고
    • Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidase
    • Hazzard, J.T., McLendon, G., Cusanovich, M.A., Das, G., Sherman, F., Tollin, G. Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidase. Biochemistry 27:4445-4451, 1988.
    • (1988) Biochemistry , vol.27 , pp. 4445-4451
    • Hazzard, J.T.1    McLendon, G.2    Cusanovich, M.A.3    Das, G.4    Sherman, F.5    Tollin, G.6
  • 55
    • 0030045925 scopus 로고    scopus 로고
    • Binding dynamics and electron transfer between plastocyanin and photosystem I
    • Drepper, F., Hippler, M., Nitschke, W., Haeechnel, W. Binding dynamics and electron transfer between plastocyanin and photosystem I. Biochemistry 35:1282-1295, 1996.
    • (1996) Biochemistry , vol.35 , pp. 1282-1295
    • Drepper, F.1    Hippler, M.2    Nitschke, W.3    Haeechnel, W.4
  • 57
    • 0028177551 scopus 로고
    • 553 from Desulfovibrio vulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase
    • 553 from Desulfovibrio vulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase. Eur. J. Biochem. 221:821-829, 1994.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 821-829
    • Verhagen, M.F.J.M.1    Wolbert, R.B.G.2    Hagen, W.R.3
  • 58
    • 0020585019 scopus 로고
    • Kinetic properties of hydrogenase isolated from Desulfovibrio vulgaris (Hildenborough)
    • Grande, H.J., Van Berkel-Arts, A., Bregh, J., VanDijk, K., Veeger, C. Kinetic properties of hydrogenase isolated from Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 131:81-88, 1983.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 81-88
    • Grande, H.J.1    Van Berkel-Arts, A.2    Bregh, J.3    VanDijk, K.4    Veeger, C.5
  • 59
    • 0028908139 scopus 로고
    • Cooperativity in enzyme function: Equilibrium and kinetic
    • Neet, K.E. Cooperativity in enzyme function: equilibrium and kinetic. Methods Enzymol. 249:519-567, 1995.
    • (1995) Methods Enzymol. , vol.249 , pp. 519-567
    • Neet, K.E.1
  • 64
    • 0026111005 scopus 로고
    • 3. Structural hypothesis on an intramolecular electron transfer pathway within a tetra-heme cytochrome
    • 3. Structural hypothesis on an intramolecular electron transfer pathway within a tetra-heme cytochrome. J. Mol. Recogn. 4:27-33, 1991.
    • (1991) J. Mol. Recogn. , vol.4 , pp. 27-33
    • Dolla, A.1    Guerlesquin, F.2    Bruschi, M.3    Haser, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.