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Volumn 41, Issue 6, 2008, Pages 730-738

Protein control of true, gated, and coupled electron transfer reactions

Author keywords

[No Author keywords available]

Indexed keywords

AMINE DEHYDROGENASE; BACTERIAL PROTEIN; COPPER; CYTOCHROME C; CYTOCHROME C(551); OXIDOREDUCTASE; WATER;

EID: 47249166440     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar700252c     Document Type: Review
Times cited : (85)

References (49)
  • 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
    • 0033975320 scopus 로고    scopus 로고
    • What controls the rates of interprotein electron-transfer reactions
    • Davidson, V. L. What controls the rates of interprotein electron-transfer reactions. Acc. Chem. Res. 2000, 33, 87-93.
    • (2000) Acc. Chem. Res , vol.33 , pp. 87-93
    • Davidson, V.L.1
  • 3
    • 0029806796 scopus 로고    scopus 로고
    • Unraveling the kinetic complexity of interprotein electron transfer reactions
    • 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
  • 5
    • 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. Science 1992, 258, 1748-1755.
    • (1748) Science , vol.1992 , pp. 258
    • Pelletier, H.1    Kraut, J.2
  • 6
    • 3543004682 scopus 로고    scopus 로고
    • Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex
    • Toogood, H. S.; van Thiel, A.; Basran, J.; Sutcliffe, M. J.; Scrutton, N. S.; Leys, D. Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J. Biol. Chem. 2004, 279, 32904-32912.
    • (2004) J. Biol. Chem , vol.279 , pp. 32904-32912
    • Toogood, H.S.1    van Thiel, A.2    Basran, J.3    Sutcliffe, M.J.4    Scrutton, N.S.5    Leys, D.6
  • 10
    • 0028296944 scopus 로고
    • Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin, and cytochrome c551i
    • Chen, L.; Durley, R. C.; Mathews, F. S.; Davidson, V. L. Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin, and cytochrome c551i. Science 1994, 264, 86-90.
    • (1994) Science , vol.264 , pp. 86-90
    • Chen, L.1    Durley, R.C.2    Mathews, F.S.3    Davidson, V.L.4
  • 12
    • 1542328169 scopus 로고    scopus 로고
    • Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy
    • Ferrari, D.; Di Valentin, M.; Carbonera, D.; Merli, A.; Chen, Z.-W.; Mathews, F. S.; Davidson, V. L.; Rossi, G.-L. Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy. J. Biol. Inorg. Chem. 2004, 9, 231-237.
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 231-237
    • Ferrari, D.1    Di Valentin, M.2    Carbonera, D.3    Merli, A.4    Chen, Z.-W.5    Mathews, F.S.6    Davidson, V.L.7    Rossi, G.-L.8
  • 13
    • 0025733905 scopus 로고
    • Intermolecular electron transfer from quinoproteins and its relevance to biosensor technology
    • 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
  • 15
    • 0023043203 scopus 로고
    • Properties of Paracoccus denitrificans amicyanin
    • Husain, M.; Davidson, V. L.; Smith, A. J. Properties of Paracoccus denitrificans amicyanin. Biochemistry 1986, 25, 2431-2436.
    • (1986) Biochemistry , vol.25 , pp. 2431-2436
    • Husain, M.1    Davidson, V.L.2    Smith, A.J.3
  • 16
    • 0022998580 scopus 로고
    • Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans
    • Husain, M.; Davidson, V. L. Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans. J. Biol. Chem. 1986, 261, 8577-8580.
    • (1986) J. Biol. Chem , vol.261 , pp. 8577-8580
    • Husain, M.1    Davidson, V.L.2
  • 17
    • 0030669092 scopus 로고    scopus 로고
    • Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein 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 protein 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
  • 18
    • 0034254541 scopus 로고    scopus 로고
    • Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge
    • Zhu, Z.; Jones, L. H.; Graichen, M. E.; Davidson, V. L. Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge. Biochemistry 2000, 39, 8830-8836.
    • (2000) Biochemistry , vol.39 , pp. 8830-8836
    • Zhu, Z.1    Jones, L.H.2    Graichen, M.E.3    Davidson, V.L.4
  • 19
    • 3242666035 scopus 로고    scopus 로고
    • Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper
    • Carrell, C. J.; Sun, D.; Jiang, S.; Davidson, V. L.; Mathews, F. S. Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper. Biochemistry 2004, 43, 9372-9380.
    • (2004) Biochemistry , vol.43 , pp. 9372-9380
    • Carrell, C.J.1    Sun, D.2    Jiang, S.3    Davidson, V.L.4    Mathews, F.S.5
  • 20
    • 0034707905 scopus 로고    scopus 로고
    • Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: Implications for predicting electron transfer pathways
    • Davidson, V. L.; Jones, L. H.; Graichen, M. E.; Zhu, Z. Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: Implications for predicting electron transfer pathways. Biochim. Biophys. Acta 2000, 1457, 27-35.
    • (2000) Biochim. Biophys. Acta , vol.1457 , pp. 27-35
    • Davidson, V.L.1    Jones, L.H.2    Graichen, M.E.3    Zhu, Z.4
  • 21
    • 0032546618 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Phe 97 to Glu in amicyanin alters the electronic coupling for interprotein electron transfer from quinol methylamine dehydrogenase
    • Davidson, V. L.; Jones, L. H.; Zhu, Z. Site-directed mutagenesis of Phe 97 to Glu in amicyanin alters the electronic coupling for interprotein 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
  • 22
    • 0037180314 scopus 로고    scopus 로고
    • Mutation of αPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin
    • Sun, D.; Chen, Z. W.; Mathews, F. S.; Davidson, V. L. Mutation of αPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin. Biochemistry 2002, 41, 13926-13933.
    • (2002) Biochemistry , vol.41 , pp. 13926-13933
    • Sun, D.1    Chen, Z.W.2    Mathews, F.S.3    Davidson, V.L.4
  • 23
    • 34547098017 scopus 로고    scopus 로고
    • Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energy
    • Ma, J. K.; Mathews, F. S.; Davidson, V. L. Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energy. Bochemistry 2007, 46, 8561-8568.
    • (2007) Bochemistry , vol.46 , pp. 8561-8568
    • Ma, J.K.1    Mathews, F.S.2    Davidson, V.L.3
  • 24
    • 33745847159 scopus 로고    scopus 로고
    • Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated
    • Ma, J. K.; Carrell, C. J.; Mathews, F. S.; Davidson, V. L. Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated. Biochemistry 2006, 45, 8284-8293.
    • (2006) Biochemistry , vol.45 , pp. 8284-8293
    • Ma, J.K.1    Carrell, C.J.2    Mathews, F.S.3    Davidson, V.L.4
  • 25
    • 18544370722 scopus 로고    scopus 로고
    • Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled
    • Sun, D.; Li, X.; Mathews, F. S.; Davidson, V. L. Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled. Biochemistry 2005, 44, 7200-7206.
    • (2005) Biochemistry , vol.44 , pp. 7200-7206
    • Sun, D.1    Li, X.2    Mathews, F.S.3    Davidson, V.L.4
  • 27
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C.; Moser, C. C.; Chen, X.; Dutton, P. L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 1999, 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 28
    • 0034712643 scopus 로고    scopus 로고
    • Effects of kinetic coupling on experimentally determined electron transfer parameters
    • Davidson, V. L. Effects of kinetic coupling on experimentally determined electron transfer parameters. Biochemistry 2000, 39, 4924-4928.
    • (2000) Biochemistry , vol.39 , pp. 4924-4928
    • Davidson, V.L.1
  • 29
    • 0037126717 scopus 로고    scopus 로고
    • Chemically gated electron transfer. A means of accelerating and regulating rates of biological electron transfer
    • Davidson, V. L. Chemically gated electron transfer. A means of accelerating and regulating rates of biological electron transfer. Biochemistry 2002, 41, 14633-14636.
    • (2002) Biochemistry , vol.41 , pp. 14633-14636
    • Davidson, V.L.1
  • 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, 13586-13592.
    • (1997) Biochemistry , vol.36 , pp. 13586-13592
    • Bishop, G.R.1    Davidson, V.L.2
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0034687156 scopus 로고    scopus 로고
    • Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue
    • Zhu, Z.; Sun, D.; Davidson, V. L. Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue. Biochemistry 2000, 39, 11184-11186.
    • (2000) Biochemistry , vol.39 , pp. 11184-11186
    • Zhu, Z.1    Sun, D.2    Davidson, V.L.3
  • 34
    • 33847023097 scopus 로고    scopus 로고
    • Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties
    • Carrell, C. J.; Ma, J. K.; Antholine, W. E.; Hosler, J. P.; Mathews, F. S.; Davidson, V. L. Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties. Biochemistry 2007, 46, 1900-1912.
    • (2007) Biochemistry , vol.46 , pp. 1900-1912
    • Carrell, C.J.1    Ma, J.K.2    Antholine, W.E.3    Hosler, J.P.4    Mathews, F.S.5    Davidson, V.L.6
  • 35
    • 0031700045 scopus 로고    scopus 로고
    • Quantum chemical calculations of the reorganization energy of blue-copper proteins
    • Olsson, M. H.; Ryde, U.; Roos, B. O. Quantum chemical calculations of the reorganization energy of blue-copper proteins. Protein Sci. 1998, 7, 2659-2668.
    • (1998) Protein Sci , vol.7 , pp. 2659-2668
    • Olsson, M.H.1    Ryde, U.2    Roos, B.O.3
  • 36
    • 0027998885 scopus 로고
    • Rack-induced bonding in blue-copper proteins
    • Malmstrom, B. G. Rack-induced bonding in blue-copper proteins. Eur. J. Biochem. 1994, 223, 711-718.
    • (1994) Eur. J. Biochem , vol.223 , pp. 711-718
    • Malmstrom, B.G.1
  • 37
    • 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
  • 38
    • 0036185564 scopus 로고    scopus 로고
    • An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins
    • Machczynski, M. C.; Gray, H. B.; Richards, J. H. An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins. J. Inorg. Biochem. 2002, 88, 375-380.
    • (2002) J. Inorg. Biochem , vol.88 , pp. 375-380
    • Machczynski, M.C.1    Gray, H.B.2    Richards, J.H.3
  • 39
    • 0037452548 scopus 로고    scopus 로고
    • Effects of engineering uphill electron transfer into the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex
    • Sun, D.; Davidson, V. L. Effects of engineering uphill electron transfer into the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex. Biochemistry 2003, 42, 1772-1776.
    • (2003) Biochemistry , vol.42 , pp. 1772-1776
    • Sun, D.1    Davidson, V.L.2
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0028900533 scopus 로고
    • Mechanistic studies of aromatic amine dehydrogenase, a tryptophan tryptophylquinone enzyme
    • Hyun, Y. L.; Davidson, V. L. Mechanistic studies of aromatic amine dehydrogenase, a tryptophan tryptophylquinone enzyme. Biochemistry 1995, 34, 816-823.
    • (1995) Biochemistry , vol.34 , pp. 816-823
    • Hyun, Y.L.1    Davidson, V.L.2
  • 43
    • 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
  • 44
    • 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
  • 45
    • 0035936584 scopus 로고    scopus 로고
    • MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127Δ-Fe-protein and the MoFe-protein
    • Chiu, H.; Peters, J. W.; Lanzilotta, W. N.; Ryle, M. J.; Seefeldt, L. C.; Howard, J. B.; Rees, D. C. MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127Δ-Fe-protein and the MoFe-protein. Biochemistry 2001, 40, 641-650.
    • (2001) Biochemistry , vol.40 , pp. 641-650
    • Chiu, H.1    Peters, J.W.2    Lanzilotta, W.N.3    Ryle, M.J.4    Seefeldt, L.C.5    Howard, J.B.6    Rees, D.C.7
  • 46
    • 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
  • 47
    • 0037031277 scopus 로고    scopus 로고
    • The roles of coenzyme A in the pyruvate:ferredoxin oxidoreductase reaction mechanism: Rate enhancement of electron transfer from a radical intermediate to an iron-sulfur cluster
    • Furdui, C.; Ragsdale, S. W. The roles of coenzyme A in the pyruvate:ferredoxin oxidoreductase reaction mechanism: Rate enhancement of electron transfer from a radical intermediate to an iron-sulfur cluster. Biochemistry 2002, 41, 9921-9937.
    • (2002) Biochemistry , vol.41 , pp. 9921-9937
    • Furdui, C.1    Ragsdale, S.W.2
  • 48
    • 34848922789 scopus 로고    scopus 로고
    • A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin
    • Ma, J. K.; Wang, Y.; Carrell, C. J.; Mathews, F. S.; Davidson, V. L. A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin. Biochemistry 2007, 46, 11137-11146.
    • (2007) Biochemistry , vol.46 , pp. 11137-11146
    • Ma, J.K.1    Wang, Y.2    Carrell, C.J.3    Mathews, F.S.4    Davidson, V.L.5
  • 49
    • 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. X. 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.X.5


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