메뉴 건너뛰기




Volumn 33, Issue 2, 2000, Pages 87-93

What controls the rates of interprotein electron-transfer reactions

Author keywords

[No Author keywords available]

Indexed keywords

AMICYANIN; AMINE DEHYDROGENASE; AZURIN; COPPER; CYTOCHROME C; HEME; PROTEIN; TRYPTOPHAN DERIVATIVE;

EID: 0033975320     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar9900616     Document Type: Article
Times cited : (130)

References (45)
  • 1
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus, R. A.; Sutin, N. Electron transfers in chemistry and biology. Biochim. Biophys. Acta 1985, 811, 265-322.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 2
    • 0016273342 scopus 로고
    • Electron transfer between biological molecules by thermally activated tunneling
    • Hopfield, J. J. Electron transfer between biological molecules by thermally activated tunneling. Proc. Natl. Acad. Sci. U.S.A. 1974, 71, 3640-3644.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 3640-3644
    • Hopfield, J.J.1
  • 4
    • 0031886681 scopus 로고    scopus 로고
    • Calculation of electron-transfer reorganizational energies using the finite difference Poisson-Boltzmann model
    • Sharp, K. A. Calculation of electron-transfer reorganizational energies using the finite difference Poisson-Boltzmann model. Biophys. J. 1998, 73, 1241-1250.
    • (1998) Biophys. J. , vol.73 , pp. 1241-1250
    • Sharp, K.A.1
  • 5
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • (a) Gray, H. B.; Winkler, J. R. Electron transfer in proteins. Annu. Rev. Biochem. 1996, 65, 537-561.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.R.2
  • 6
    • 0026434593 scopus 로고
    • Protein electron-transfer rates set by the bridging secondary and tertiary structure
    • (b) Beratan, D. N.; Betts, J. N.; Onuchic, J. N. Protein electron-transfer rates set by the bridging secondary and tertiary structure. Science 1991, 252, 1285-1288.
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 7
    • 0000517770 scopus 로고
    • Protein electron transport: Single versus multiple pathways
    • Regan, J. J.; Risser, S. M.; Beratan, D. N.; Onuchic, J. N. Protein electron transport: Single versus multiple pathways. J. Phys. Chem. 1993, 97, 13083-13088.
    • (1993) J. Phys. Chem. , vol.97 , pp. 13083-13088
    • Regan, J.J.1    Risser, S.M.2    Beratan, D.N.3    Onuchic, J.N.4
  • 8
    • 0029806796 scopus 로고    scopus 로고
    • Unraveling the kinetic complexity of interprotein electron-transfer reactions
    • (a) Davidson, V. L. Unraveling the kinetic complexity of interprotein electron-transfer reactions. Biochemistry 1996, 35, 14035-14039.
    • (1996) Biochemistry , vol.35 , pp. 14035-14039
    • Davidson, V.L.1
  • 9
    • 0344187406 scopus 로고
    • Gated electron transfer: When are observed rates controlled by conformational interconversion?
    • (b) Hoffman, B. M.; Ratner, M. A. Gated electron transfer: When are observed rates controlled by conformational interconversion? J. Am. Chem. Soc. 1987, 109, 6237-6243.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6237-6243
    • Hoffman, B.M.1    Ratner, M.A.2
  • 10
    • 33845183857 scopus 로고
    • Directional electron transfer: Conformational interconversions and their effects on observed electron-transfer rate constants
    • (c) Brunschwig, B. S.; Sutin, N. Directional electron transfer: Conformational interconversions and their effects on observed electron-transfer rate constants. J. Am. Chem. Soc. 1989, 110, 7454-7465.
    • (1989) J. Am. Chem. Soc. , vol.110 , pp. 7454-7465
    • Brunschwig, B.S.1    Sutin, N.2
  • 11
    • 0345330736 scopus 로고
    • Electron transfer in ruthenium-modified proteins
    • Winkler, J. R.; Gray, H. B. Electron transfer in ruthenium-modified proteins. Chem. Rev. 1992, 92, 369-379.
    • (1992) Chem. Rev. , vol.92 , pp. 369-379
    • Winkler, J.R.1    Gray, H.B.2
  • 12
    • 0027759655 scopus 로고
    • Binding and electron-transfer reactions between methanol dehydrogenase and its physiologic electron acceptor cytochrome c-551i. A kinetic and thermodynamic analysis
    • Harris, T. K.; Davidson, V. L. Binding and electron-transfer reactions between methanol dehydrogenase and its physiologic electron acceptor cytochrome c-551i. A kinetic and thermodynamic analysis. Biochemistry 1993, 32, 14145-14150.
    • (1993) Biochemistry , vol.32 , pp. 14145-14150
    • Harris, T.K.1    Davidson, V.L.2
  • 13
    • 0027970374 scopus 로고
    • Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: Evidence of conformationally coupled electron transfer
    • Harris, T. K.; Davidson, V. L.; Chen, L.; Mathews, F. S.; Xia, Z.-H. Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: Evidence of conformationally coupled electron transfer. Biochemistry 1994, 33, 12600-12608.
    • (1994) Biochemistry , vol.33 , pp. 12600-12608
    • Harris, T.K.1    Davidson, V.L.2    Chen, L.3    Mathews, F.S.4    Xia, Z.-H.5
  • 14
    • 0028296944 scopus 로고
    • Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin and cytochrome c-551i
    • Chen, L.; Durley, R.; Mathews, F. S.; Davidson, V. L. Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin and cytochrome c-551i. Science 1994, 264, 86-90.
    • (1994) Science , vol.264 , pp. 86-90
    • Chen, L.1    Durley, R.2    Mathews, F.S.3    Davidson, V.L.4
  • 16
    • 0025149403 scopus 로고
    • Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation
    • Van Spanning, R. J. M.; Wansell, C. W.; Reijnders, W. N. M.; Oltmann, L. F.; Stouthamer, A. H. Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett. 1990, 275, 217-220.
    • (1990) FEBS Lett. , vol.275 , pp. 217-220
    • Van Spanning, R.J.M.1    Wansell, C.W.2    Reijnders, W.N.M.3    Oltmann, L.F.4    Stouthamer, A.H.5
  • 17
    • 0023812932 scopus 로고
    • Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans
    • Gray, K. A.; Davidson, V. L.; Knaff, D. B. Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans. J. Biol. Chem. 1988, 263, 13987-13990.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13987-13990
    • Gray, K.A.1    Davidson, V.L.2    Knaff, D.B.3
  • 18
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties and physiological role
    • (a) Husain, M.; Davidson, V. L. An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties and physiological role. J. Biol. Chem. 1985, 260, 14626-14629.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 19
    • 0023003367 scopus 로고
    • Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans
    • (b) Gray, K. A.; Knaff, D. B.; Husain, M.; Davidson, V. L. Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans. FEBS Lett. 1986, 207, 239-242.
    • (1986) FEBS Lett. , vol.207 , pp. 239-242
    • Gray, K.A.1    Knaff, D.B.2    Husain, M.3    Davidson, V.L.4
  • 20
    • 0025733905 scopus 로고
    • Intermolecular electron transfer from quinoproteins and its relevance to biosensor technology
    • (c) Davidson, V. L.; Jones, L. H. Intermolecular electron transfer from quinoproteins and its relevance to biosensor technology. Anal. Chim. Acta 1991, 249, 235-240.
    • (1991) Anal. Chim. Acta , vol.249 , pp. 235-240
    • Davidson, V.L.1    Jones, L.H.2
  • 21
    • 0028884223 scopus 로고
    • Complex formation with methylamine dehydrogenase affects the pathway of electron transfer from amicyanin to cytochrome c-551i
    • (d) Davidson, V. L.; Jones, L. H. Complex formation with methylamine dehydrogenase affects the pathway of electron transfer from amicyanin to cytochrome c-551i. J. Biol. Chem. 1995, 270, 23941-23943.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23941-23943
    • Davidson, V.L.1    Jones, L.H.2
  • 22
    • 0032497926 scopus 로고    scopus 로고
    • Molecular basis for interprotein complex-dependent effects on the redox potential of amicyanin
    • Zhu, Z.; Cunane, L. M.; Chen, Z.-W.; Durley, R. C. E.; Mathews, F. S.; Davidson, V. L. Molecular basis for interprotein complex-dependent effects on the redox potential of amicyanin. Biochemistry 1998, 37, 17128-17136.
    • (1998) Biochemistry , vol.37 , pp. 17128-17136
    • Zhu, Z.1    Cunane, L.M.2    Chen, Z.-W.3    Durley, R.C.E.4    Mathews, F.S.5    Davidson, V.L.6
  • 23
    • 0029122664 scopus 로고
    • Electron-transfer reactions between aromatic amine dehydrogenase and azurin
    • Hyun, Y.-L; Davidson V. L. Electron-transfer reactions between aromatic amine dehydrogenase and azurin. Biochemistry 1995, 34, 12249-12254.
    • (1995) Biochemistry , vol.34 , pp. 12249-12254
    • Hyun, Y.-L.1    Davidson, V.L.2
  • 24
    • 0032486474 scopus 로고    scopus 로고
    • Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity
    • Zhu, Z.; Davidson, V. L. Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity. J. Biol. Chem. 1998, 273, 14254-14260.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14254-14260
    • Zhu, Z.1    Davidson, V.L.2
  • 26
    • 0032483134 scopus 로고    scopus 로고
    • Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin
    • Bishop, G. R.; Davidson, V. L Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin. Biochemistry 1998, 37, 11026-11032.
    • (1998) Biochemistry , vol.37 , pp. 11026-11032
    • Bishop, G.R.1    Davidson, V.L.2
  • 27
    • 0000947245 scopus 로고
    • Free energy dependence of the electron-transfer reaction between methylamine dehydrogenase and amicyanin
    • Brooks, H. B.; Davidson, V. L. Free energy dependence of the electron-transfer reaction between methylamine dehydrogenase and amicyanin. J. Am. Chem. Soc. 1994, 116, 11201-11202.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11201-11202
    • Brooks, H.B.1    Davidson, V.L.2
  • 28
    • 0028360177 scopus 로고
    • Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin
    • Brooks, H. B.; Davidson, V. L. Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin. Biochemistry 1994, 33, 5696-5701.
    • (1994) Biochemistry , vol.33 , pp. 5696-5701
    • Brooks, H.B.1    Davidson, V.L.2
  • 29
    • 0029098408 scopus 로고
    • Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer
    • Bishop, G. R.; Davidson, V. L Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer. Biochemistry 1995, 34, 12082-12086.
    • (1995) Biochemistry , vol.34 , pp. 12082-12086
    • Bishop, G.R.1    Davidson, V.L.2
  • 30
    • 0030729454 scopus 로고    scopus 로고
    • Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron-transfer reaction
    • Bishop, G. R.; Davidson, V. L. Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron-transfer reaction. Biochemistry 1997, 36, 3586-13592.
    • (1997) Biochemistry , vol.36 , pp. 3586-13592
    • Bishop, G.R.1    Davidson, V.L.2
  • 31
    • 0030669092 scopus 로고    scopus 로고
    • Factors which stabilize the methylamine dehydrogenase-amicyanin electron-transfer complex revealed by site-directed mutagenesis
    • Davidson, V. L.; Jones, L. H.; Graichen, M. E.; Mathews, F. S.; Hosler, J. P. Factors which stabilize the methylamine dehydrogenase-amicyanin electron-transfer complex revealed by site-directed mutagenesis. Biochemistry 1997, 36, 12733-12738.
    • (1997) Biochemistry , vol.36 , pp. 12733-12738
    • Davidson, V.L.1    Jones, L.H.2    Graichen, M.E.3    Mathews, F.S.4    Hosler, J.P.5
  • 32
    • 0032546618 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Phe 97 of amicyanin alters the electronic coupling for inter-protein electron transfer from quinol methylamine dehydrogenase
    • Davidson, V. L.; Jones, L. H.; Zhu, Z. Site-directed mutagenesis of Phe 97 of amicyanin alters the electronic coupling for inter-protein electron transfer from quinol methylamine dehydrogenase. Biochemistry 1998, 37, 7371-7377.
    • (1998) Biochemistry , vol.37 , pp. 7371-7377
    • Davidson, V.L.1    Jones, L.H.2    Zhu, Z.3
  • 33
    • 0030037410 scopus 로고    scopus 로고
    • Electron transfer from copper to heme within the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex
    • Davidson, V. L.; Jones, L H. Electron transfer from copper to heme within the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex. Biochemistry 1996, 35, 8120-8125.
    • (1996) Biochemistry , vol.35 , pp. 8120-8125
    • Davidson, V.L.1    Jones, L.H.2
  • 34
    • 0032829691 scopus 로고    scopus 로고
    • Gated and ungated electron-transfer reactions from aromatic amine dehydrogenase to azurin
    • Hyun, Y.-L.; Zhu, Z.; Davidson, V. L. Gated and ungated electron-transfer reactions from aromatic amine dehydrogenase to azurin. J. Biol. Chem. 1999, 274, 29081-29086.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29081-29086
    • Hyun, Y.-L.1    Zhu, Z.2    Davidson, V.L.3
  • 35
    • 0032488605 scopus 로고    scopus 로고
    • Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by MgATP
    • Lanzilotta, W. N.; Parker, V. D.; Seefeldt, L. C. Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by MgATP. Biochemistry 1998, 37, 399-407.
    • (1998) Biochemistry , vol.37 , pp. 399-407
    • Lanzilotta, W.N.1    Parker, V.D.2    Seefeldt, L.C.3
  • 36
    • 0021115292 scopus 로고
    • The ionic strength dependence of the rate of a reaction between two large proteins with a dipole moment
    • Van Leeuwen, J. W. The ionic strength dependence of the rate of a reaction between two large proteins with a dipole moment. Biochim. Biophys. Acta 1983, 743, 408-421.
    • (1983) Biochim. Biophys. Acta , vol.743 , pp. 408-421
    • Van Leeuwen, J.W.1
  • 37
    • 0038235125 scopus 로고    scopus 로고
    • Effects of viscosity on the kinetics of the electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin
    • Ivkovic-Jensen, M. M.; Kostic, N. M. Effects of viscosity on the kinetics of the electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin. Biochemistry 1997, 36, 8135-8144.
    • (1997) Biochemistry , vol.36 , pp. 8135-8144
    • Ivkovic-Jensen, M.M.1    Kostic, N.M.2
  • 38
    • 0001184693 scopus 로고    scopus 로고
    • Electron transfer from flavin to iron in the Pseudomonas oleovorans rebredoxin reductase-rubredoxin electron-transfer complex
    • Lee, H. J.; Basran, J.; Scrutton, N. S. Electron transfer from flavin to iron in the Pseudomonas oleovorans rebredoxin reductase-rubredoxin electron-transfer complex. Biochemistry 1998, 37, 15513-15522.
    • (1998) Biochemistry , vol.37 , pp. 15513-15522
    • Lee, H.J.1    Basran, J.2    Scrutton, N.S.3
  • 39
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron-transfer partners, cytochrome c peroxidase and cytochrome c
    • Pelletier, H.; Kraut, J. Crystal structure of a complex between electron-transfer partners, cytochrome c peroxidase and cytochrome c. Science1992, 258, 1748-1755.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 40
    • 0033602997 scopus 로고    scopus 로고
    • Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase
    • Mei, H.; Wang, K.; Peffer, N.; Weatherly, G.; Cohen, D. S.; Miller, M.; Pielak, G.; Durham, B.; Millett, F. Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase. Biochemistry 1999, 38, 6846-6854.
    • (1999) Biochemistry , vol.38 , pp. 6846-6854
    • Mei, H.1    Wang, K.2    Peffer, N.3    Weatherly, G.4    Cohen, D.S.5    Miller, M.6    Pielak, G.7    Durham, B.8    Millett, F.9
  • 42
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • (b) Iwata, S.; Ostermeier, C.; Ludwig, B.; Michel, H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 1995, 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 44
    • 0033580880 scopus 로고    scopus 로고
    • Structure of Escherichia colifumarate reductase respiratory complex
    • (d) Iverson T. M.; Luna-chavez, C.; Cecchini, G.; Rees, D. C. Structure of Escherichia colifumarate reductase respiratory complex. Science 1999, 284, 1961-1966.
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 45
    • 0025785660 scopus 로고
    • A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
    • McIntire, W. S.; Wemmer, D. E.; Christoserdov, A. Y.; Lindstrom, M. E. A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science 1991, 252, 817-824.
    • (1991) Science , vol.252 , pp. 817-824
    • McIntire, W.S.1    Wemmer, D.E.2    Christoserdov, A.Y.3    Lindstrom, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.