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Volumn 78, Issue 2, 2000, Pages 1001-1009

Voltammetry of a flavocytochrome c3: The lowest potential heme modulates fumarate reduction rates

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME; FUMARIC ACID; GOLD; GRAPHITE; HEME;

EID: 0034036513     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76658-6     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0021506235 scopus 로고
    • Surface modifiers for the promotion of direct electrochemistry of cytochrome c
    • Allen, P. M., H. A. O. Hill, and N. J. Walton. 1984. Surface modifiers for the promotion of direct electrochemistry of cytochrome c. J. Electroanal. Chem. 178:69-86.
    • (1984) J. Electroanal. Chem. , vol.178 , pp. 69-86
    • Allen, P.M.1    Hill, H.A.O.2    Walton, N.J.3
  • 2
    • 0001519894 scopus 로고
    • Probing metalloproteins by voltammetry
    • Armstrong, F. A. 1990. Probing metalloproteins by voltammetry. Struct. Bond. 72:137-221.
    • (1990) Struct. Bond. , vol.72 , pp. 137-221
    • Armstrong, F.A.1
  • 3
    • 33846281497 scopus 로고    scopus 로고
    • Reactions of complex metalloproteins studied by protein-film voltammetry
    • Armstrong, F. A., H. A. Heering, and J. Hirst. 1997. Reactions of complex metalloproteins studied by protein-film voltammetry. Chem. Soc. Rev. 26:169-179.
    • (1997) Chem. Soc. Rev. , vol.26 , pp. 169-179
    • Armstrong, F.A.1    Heering, H.A.2    Hirst, J.3
  • 7
    • 0000765392 scopus 로고
    • Voltammetric characterization of rapid and reversible binding of an exogenous thiolate ligand at a [4Fe-4S] cluster in Ferredoxin III from Desulfovibrio africanus
    • Butt, J. N., A. Sucheta, F. A. Armstrong, J. Breton, A. J. Thomson, and E. C. Hatchikian. 1993. Voltammetric characterization of rapid and reversible binding of an exogenous thiolate ligand at a [4Fe-4S] cluster in Ferredoxin III from Desulfovibrio africanus. J. Am. Chem. Soc. 115:1413-1421.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1413-1421
    • Butt, J.N.1    Sucheta, A.2    Armstrong, F.A.3    Breton, J.4    Thomson, A.J.5    Hatchikian, E.C.6
  • 8
    • 0018115212 scopus 로고
    • Protein thiolation and reversible protein-protein conjugation
    • Carlsson, J., H. Drevin, and R. Axén. 1978. Protein thiolation and reversible protein-protein conjugation. Biochem. J. 173:723-737.
    • (1978) Biochem. J. , vol.173 , pp. 723-737
    • Carlsson, J.1    Drevin, H.2    Axén, R.3
  • 10
    • 0026108980 scopus 로고
    • Free energy and temperature dependence of electron transfer at the metal-electrolyte interface
    • Chidsey, C. E. D. 1991. Free energy and temperature dependence of electron transfer at the metal-electrolyte interface. Science. 251: 919-922.
    • (1991) Science. , vol.251 , pp. 919-922
    • Chidsey, C.E.D.1
  • 11
    • 0026867707 scopus 로고
    • Voltammetry of covalently immobilized cytochrome c on self-assembled monolayer electrodes
    • Collison, M., E. F. Bowden, and M. J. Tarlov. 1992. Voltammetry of covalently immobilized cytochrome c on self-assembled monolayer electrodes. Langmuir. 8:1247-1250.
    • (1992) Langmuir. , vol.8 , pp. 1247-1250
    • Collison, M.1    Bowden, E.F.2    Tarlov, M.J.3
  • 14
    • 0029804670 scopus 로고    scopus 로고
    • Film architecture in biomolecular assemblies. Effect of linker of the orientation of genetically engineered surface-bound proteins
    • Firestone, M. A., M. L. Shank, S. G. Sligar, and P. W. Bohn. 1996. Film architecture in biomolecular assemblies. Effect of linker of the orientation of genetically engineered surface-bound proteins. J. Am. Chem. Soc. 118:9033-9041.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9033-9041
    • Firestone, M.A.1    Shank, M.L.2    Sligar, S.G.3    Bohn, P.W.4
  • 15
    • 0001678195 scopus 로고    scopus 로고
    • Interpreting the catalytic voltammetry of electroactive enzymes adsorbed on electrodes
    • Heering, H. A., J. Hirst, and F. A. Armstrong. 1998. Interpreting the catalytic voltammetry of electroactive enzymes adsorbed on electrodes. J. Phys. Chem. B. 102:6889-6902.
    • (1998) J. Phys. Chem. B. , vol.102 , pp. 6889-6902
    • Heering, H.A.1    Hirst, J.2    Armstrong, F.A.3
  • 16
    • 0031451230 scopus 로고    scopus 로고
    • Direct detection and measurement of electron relays in a multicentered enzyme: Voltammetry of electrode-surface films of E. Coli fumarate reductase, an iron-sulfur flavoprotein
    • Heering, H. A., J. H. Weiner, and F. A. Armstrong. 1997. Direct detection and measurement of electron relays in a multicentered enzyme: voltammetry of electrode-surface films of E. coli fumarate reductase, an iron-sulfur flavoprotein. J. Am. Chem. Soc. 48:11628-11638.
    • (1997) J. Am. Chem. Soc. , vol.48 , pp. 11628-11638
    • Heering, H.A.1    Weiner, J.H.2    Armstrong, F.A.3
  • 17
    • 0032558152 scopus 로고    scopus 로고
    • Kinetics and mechanism of redox-coupled, long-range proton transfer in an iron-sulfur protein. Investigation by fast-scan protein-film voltammetry
    • Hirst, J., J. L. C. Duff, G. N. L. Jameson, M. A. Kemper, B. K. Burgess, and F. A. Armstrong. 1998a. Kinetics and mechanism of redox-coupled, long-range proton transfer in an iron-sulfur protein. Investigation by fast-scan protein-film voltammetry. J. Am. Chem. Soc. 120:7085-7094.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7085-7094
    • Hirst, J.1    Duff, J.L.C.2    Jameson, G.N.L.3    Kemper, M.A.4    Burgess, B.K.5    Armstrong, F.A.6
  • 18
    • 0032567224 scopus 로고    scopus 로고
    • Very rapid cooperative two electron/two proton redox reactions of [3Fe-4S] Clusters: Detection and analysis by protein film voltammetry
    • Hirst, J., G. N. L. Jameson, J. W. A. Allen, and F. A. Armstrong. 1998b. Very rapid cooperative two electron/two proton redox reactions of [3Fe-4S] Clusters: detection and analysis by protein film voltammetry J. Am. Chem. Soc. 120:11994-11999.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11994-11999
    • Hirst, J.1    Jameson, G.N.L.2    Allen, J.W.A.3    Armstrong, F.A.4
  • 19
    • 15844392907 scopus 로고    scopus 로고
    • Electrocatalytic voltammetry of succinate dehydrogenase: Direct quantification of the catalytic properties of a complex electron-transport enzyme
    • Hirst, J., A. Sucheta, B. A. C. Ackrell, and F. A. Armstrong. 1996. Electrocatalytic voltammetry of succinate dehydrogenase: direct quantification of the catalytic properties of a complex electron-transport enzyme. J. Am. Chem. Soc. 118:5031-5038.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5031-5038
    • Hirst, J.1    Sucheta, A.2    Ackrell, B.A.C.3    Armstrong, F.A.4
  • 20
    • 0030611275 scopus 로고    scopus 로고
    • The 2.8 Å structure of the hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
    • Igarashi, N., H. Moriyama, T. Fujiwara, Y. Fukomori, and N. Tanaka. 1997. The 2.8 Å structure of the hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nat. Struct. Biol. 4:276-284.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 276-284
    • Igarashi, N.1    Moriyama, H.2    Fujiwara, T.3    Fukomori, Y.4    Tanaka, N.5
  • 21
    • 37049082457 scopus 로고
    • Direct electron transfer reactions of glucose oxidase immobilized at a self-assembled monolayer
    • Jiang, L., C. J. McNeil, and J. M. Cooper. 1995. Direct electron transfer reactions of glucose oxidase immobilized at a self-assembled monolayer. J. Chem. Soc. Chem. Commun. 1293-1295.
    • (1995) J. Chem. Soc. Chem. Commun. , pp. 1293-1295
    • Jiang, L.1    McNeil, C.J.2    Cooper, J.M.3
  • 22
    • 0017863234 scopus 로고
    • Preparation of protein conjugates via intermolecular disulfide bond formation
    • King, T. P., Y. Li, and L. Kochoumian. 1978. Preparation of protein conjugates via intermolecular disulfide bond formation. Biochemistry. 17:1499-1506.
    • (1978) Biochemistry , vol.17 , pp. 1499-1506
    • King, T.P.1    Li, Y.2    Kochoumian, L.3
  • 23
    • 0002709238 scopus 로고
    • The effect of orientation of cytochrome c molecules covalently attached to the electrode surface upon their electrochemical activity
    • Kuznetsov, B. A., N. A. Byzova, and G. P. Shumakovich. 1994. The effect of orientation of cytochrome c molecules covalently attached to the electrode surface upon their electrochemical activity. J. Electroanal. Chem. 371:85-92.
    • (1994) J. Electroanal. Chem. , vol.371 , pp. 85-92
    • Kuznetsov, B.A.1    Byzova, N.A.2    Shumakovich, G.P.3
  • 24
    • 33845281250 scopus 로고
    • Fundamental studies of the chemisorption of organosulfur compounds on Au(111). Implications for molecular self-assembly on gold surfaces
    • Nuzzo, R. G., B. R. Zegarski, and L. H. Dubois, 1987. Fundamental studies of the chemisorption of organosulfur compounds on Au(111). Implications for molecular self-assembly on gold surfaces. J. Am. Chem. Soc. 109:733-740.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 733-740
    • Nuzzo, R.G.1    Zegarski, B.R.2    Dubois, L.H.3
  • 25
    • 0015223578 scopus 로고
    • Reaction of tobacco mosaic virus with a thiol-containing imodoester and a possible application to x-ray diffraction analysis
    • Perham, N. R., and J. O. Thomas. 1971. Reaction of tobacco mosaic virus with a thiol-containing imodoester and a possible application to x-ray diffraction analysis. J. Mol Biol. 62:415-418.
    • (1971) J. Mol Biol. , vol.62 , pp. 415-418
    • Perham, N.R.1    Thomas, J.O.2
  • 26
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siècle
    • Saraste, M. 1999. Oxidative phosphorylation at the fin de siècle. Science. 283:1488-1493.
    • (1999) Science. , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 27
    • 0029034904 scopus 로고
    • Enzyme or protein immobilization methods for applications in biosensor design
    • Scouten, W. H., J. H. T. Luong, and R. S. Brown. 1995. Enzyme or protein immobilization methods for applications in biosensor design. TIBTECH .13:178-185.
    • (1995) TIBTECH , vol.13 , pp. 178-185
    • Scouten, W.H.1    Luong, J.H.T.2    Brown, R.S.3
  • 29
    • 0028513774 scopus 로고
    • Site-specific immobilization of molecularly engineered dihydrofolate reductase to gold surfaces
    • Vigmond, S. J., M. Iwakura, F. Mizutani, and T. Katsura. 1994. Site-specific immobilization of molecularly engineered dihydrofolate reductase to gold surfaces. Langmuir. 10:2860-2862.
    • (1994) Langmuir. , vol.10 , pp. 2860-2862
    • Vigmond, S.J.1    Iwakura, M.2    Mizutani, F.3    Katsura, T.4
  • 30
    • 0001554306 scopus 로고
    • Voltammetry of redox-active groups irreversibly adsorbed onto electrodes. Treatment using the Marcus relation between rate and overpotential
    • Weber, K., and S. E. Creager. 1994. Voltammetry of redox-active groups irreversibly adsorbed onto electrodes. Treatment using the Marcus relation between rate and overpotential. Anal. Chem. 66:3164-3172.
    • (1994) Anal. Chem. , vol.66 , pp. 3164-3172
    • Weber, K.1    Creager, S.E.2
  • 31
    • 25744445484 scopus 로고
    • Microvoltammetric electrodes
    • Wightman, R. M. 1981. Microvoltammetric electrodes. Anal. Chem. 53: 1125A-1134A.
    • (1981) Anal. Chem. , vol.53
    • Wightman, R.M.1
  • 32
    • 0015499006 scopus 로고
    • The conversion of tryptophan to 2-thioltryptophan in peptides and proteins
    • Wilchek, M., and T. Miron. 1972. The conversion of tryptophan to 2-thioltryptophan in peptides and proteins. Biochem. Biophys. Res. Commun. 47:1015-1020.
    • (1972) Biochem. Biophys. Res. Commun. , vol.47 , pp. 1015-1020
    • Wilchek, M.1    Miron, T.2
  • 33
    • 0642375842 scopus 로고    scopus 로고
    • Photoswitchable biomaterials: En route to optobioelectronic systems
    • Willner, I. 1997. Photoswitchable biomaterials: en route to optobioelectronic systems. Acc. Chem. Res. 30:347-356.
    • (1997) Acc. Chem. Res. , vol.30 , pp. 347-356
    • Willner, I.1
  • 34
    • 1842365512 scopus 로고    scopus 로고
    • Molecular orientation distributions in protein films. 2. Site-directed immobilization of yeast cytochrome c on thiol capped self-assembled monolayers
    • Wood, L. L., S-S. Cheng, P. L. Edmiston, and S. S. Saavedra. 1997. Molecular orientation distributions in protein films. 2. Site-directed immobilization of yeast cytochrome c on thiol capped self-assembled monolayers. J. Am. Chem. Soc. 119:571-576.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 571-576
    • Wood, L.L.1    Cheng, S.-S.2    Edmiston, P.L.3    Saavedra, S.S.4


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