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Volumn 46, Issue 28, 2007, Pages 8263-8272

Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: Mutations near the high-affinity cytochrome c binding site

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLOGRAPHIC STRUCTURE; CYTOCHROME C PEROXIDASE (CCP); HEXACOORDINATE HEME SPECIES; MICHAELIS CONSTANT;

EID: 34447547742     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700623u     Document Type: Article
Times cited : (19)

References (50)
  • 1
    • 0014027714 scopus 로고
    • Cytochrome c peroxidase, a mitochondrial enzyme of yeast
    • Yonetani, T., and Ohnisi, T. (1966) Cytochrome c peroxidase, a mitochondrial enzyme of yeast, J. Biol. Chem. 241, 2983-2984.
    • (1966) J. Biol. Chem , vol.241 , pp. 2983-2984
    • Yonetani, T.1    Ohnisi, T.2
  • 2
    • 0014010710 scopus 로고
    • Studies on cytochrome c peroxidase IV. A comparison of peroxide-induced complexes of horseradish and cytochrome c peroxidases
    • Yonetani, T. (1966) Studies on cytochrome c peroxidase IV. A comparison of peroxide-induced complexes of horseradish and cytochrome c peroxidases, J. Biol. Chem. 241, 2562-2571.
    • (1966) J. Biol. Chem , vol.241 , pp. 2562-2571
    • Yonetani, T.1
  • 4
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution
    • Finzel, B. C., Poulos, T. L., and Kraut, J. (1984) Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution, J. Biol. Chem. 259, 13027-13036.
    • (1984) J. Biol. Chem , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 5
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T. L., and Kraut, J. (1980) The stereochemistry of peroxidase catalysis, J. Biol. Chem. 255, 8199-8205.
    • (1980) J. Biol. Chem , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2
  • 6
    • 0027421337 scopus 로고
    • Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I
    • Erman, J. E., Vitello, L. B., Miller, M. A., Shaw, A., Brown, K. A., and Kraut, J. (1993) Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I, Biochemistry 32, 9798-9806.
    • (1993) Biochemistry , vol.32 , pp. 9798-9806
    • Erman, J.E.1    Vitello, L.B.2    Miller, M.A.3    Shaw, A.4    Brown, K.A.5    Kraut, J.6
  • 7
    • 0001102428 scopus 로고    scopus 로고
    • Theory and practice of electron transfer within protein-protein complexes: Application to the multidomain binding of cytochrome c by cytochrome c peroxidase
    • Nocek, J. M., Zhou, J. S., De Forest, S., Priyadarshi, S., Beratan, D. N., Onuchic, J. N., and Hoffman, B. M. (1996) Theory and practice of electron transfer within protein-protein complexes: Application to the multidomain binding of cytochrome c by cytochrome c peroxidase, Chem. Rev. 96, 2459-2489.
    • (1996) Chem. Rev , vol.96 , pp. 2459-2489
    • Nocek, J.M.1    Zhou, J.S.2    De Forest, S.3    Priyadarshi, S.4    Beratan, D.N.5    Onuchic, J.N.6    Hoffman, B.M.7
  • 8
    • 0004177528 scopus 로고    scopus 로고
    • Bendal, D. S, Ed, Bios Scientific Publishers, Oxford, U.K
    • Bendal, D. S., Ed. (1996) Protein electron transfer, Bios Scientific Publishers, Oxford, U.K.
    • (1996) Protein electron transfer
  • 9
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c
    • Pelletier, H., and Kraut, J. (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c, Science 258, 1748-1755.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 10
    • 0002305987 scopus 로고    scopus 로고
    • Protein-protein complexes formed by electron transfer proteins
    • Kleanthous, C, Ed, pp, Oxford University Press, Oxford, U.K
    • Mathews, F. S., Mauk, A. G., and Moore, G. R. (2000) Protein-protein complexes formed by electron transfer proteins, in Protein-protein recognition (Kleanthous, C., Ed.) pp 60-101, Oxford University Press, Oxford, U.K.
    • (2000) Protein-protein recognition , pp. 60-101
    • Mathews, F.S.1    Mauk, A.G.2    Moore, G.R.3
  • 11
    • 0037014127 scopus 로고    scopus 로고
    • Yeast cytochrome c peroxidase: Mechanistic studies via protein engineering
    • Erman, J. E., and Vitello, L. B. (2002) Yeast cytochrome c peroxidase: Mechanistic studies via protein engineering, Biochim. Biophys. Acta 1597, 193-220.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 193-220
    • Erman, J.E.1    Vitello, L.B.2
  • 12
    • 0017369353 scopus 로고
    • Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase
    • Kang, C. H., Ferguson-Miller, S., and Margoliash, E. (1977) Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase, J. Biol. Chem. 252, 919-926.
    • (1977) J. Biol. Chem , vol.252 , pp. 919-926
    • Kang, C.H.1    Ferguson-Miller, S.2    Margoliash, E.3
  • 13
    • 0020479811 scopus 로고
    • The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism
    • Kang, D. S., and Erman, J. E. (1982) The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism, J. Biol. Chem. 257, 12775-12779.
    • (1982) J. Biol. Chem , vol.257 , pp. 12775-12779
    • Kang, D.S.1    Erman, J.E.2
  • 14
    • 0024040620 scopus 로고
    • Brownian dynamics of cytochrome c and cytochrome c peroxidase association
    • Northrup, S. H., Boles, J. O., and Reynolds, J. C. L. (1988) Brownian dynamics of cytochrome c and cytochrome c peroxidase association, Science 241, 67-70.
    • (1988) Science , vol.241 , pp. 67-70
    • Northrup, S.H.1    Boles, J.O.2    Reynolds, J.C.L.3
  • 15
    • 0019321862 scopus 로고
    • A hypothetical model of the cytochrome c peroxidase·cytochrome c electron transfer complex
    • Poulos, T. L., and Kraut, J. (1980) A hypothetical model of the cytochrome c peroxidase·cytochrome c electron transfer complex, J. Biol. Chem. 255, 10322-10330.
    • (1980) J. Biol. Chem , vol.255 , pp. 10322-10330
    • Poulos, T.L.1    Kraut, J.2
  • 16
    • 0001607931 scopus 로고
    • Heme enzyme structure and function
    • Poulos, T. L., and Finzel, B. C. (1984) Heme enzyme structure and function, Pept. Protein Rev. 4, 115-171.
    • (1984) Pept. Protein Rev , vol.4 , pp. 115-171
    • Poulos, T.L.1    Finzel, B.C.2
  • 17
    • 34447528136 scopus 로고
    • Computer modeling of yeast iso-1 cytochrome c-yeast cytochrome c peroxidase complexes
    • Lum, V. R., Brayer, G. D., Louie, G. V., Smith, M., and Mauk, A. G. (1987) Computer modeling of yeast iso-1 cytochrome c-yeast cytochrome c peroxidase complexes, Protein Struct., Folding, Des. 2, 143-150.
    • (1987) Protein Struct., Folding, Des , vol.2 , pp. 143-150
    • Lum, V.R.1    Brayer, G.D.2    Louie, G.V.3    Smith, M.4    Mauk, A.G.5
  • 18
    • 0021799192 scopus 로고
    • Structure of an electron transfer complex. II. Chemical modification of carboxyl groups of cytochrome c peroxidase in presence and absence of cytochrome c
    • Bechtold, R., and Bosshard, H. R. (1985) Structure of an electron transfer complex. II. Chemical modification of carboxyl groups of cytochrome c peroxidase in presence and absence of cytochrome c, J. Biol. Chem. 260, 5191-5200.
    • (1985) J. Biol. Chem , vol.260 , pp. 5191-5200
    • Bechtold, R.1    Bosshard, H.R.2
  • 19
    • 0027453442 scopus 로고
    • Cytochrome c peroxidase binds two molecules of cytochrome c: Evidence for a low-affinity, electron-transfer-active site on cytochrome c peroxidase
    • Stemp, E. D. A., and Hoffman, B. M. (1993) Cytochrome c peroxidase binds two molecules of cytochrome c: Evidence for a low-affinity, electron-transfer-active site on cytochrome c peroxidase, Biochemistry 32, 10848-10865.
    • (1993) Biochemistry , vol.32 , pp. 10848-10865
    • Stemp, E.D.A.1    Hoffman, B.M.2
  • 20
    • 0028062898 scopus 로고
    • Proton linkage in formation of the cytochrome c-cytochrome c peroxidase complex: Electrostatic properties of the high- and low-affinity cytochrome c binding sites on the peroxidase
    • Mauk, M. R., Ferrer, J. C., and Mauk, A. G. (1994) Proton linkage in formation of the cytochrome c-cytochrome c peroxidase complex: Electrostatic properties of the high- and low-affinity cytochrome c binding sites on the peroxidase, Biochemistry 33, 12609-12614.
    • (1994) Biochemistry , vol.33 , pp. 12609-12614
    • Mauk, M.R.1    Ferrer, J.C.2    Mauk, A.G.3
  • 21
    • 0026340012 scopus 로고
    • Effects of surface amino acid replacements in cytochrome c peroxidase on complex formation with cytochrome c
    • Corin, A. F., McLendon, G., Zhang, Q., Hake, R. A., Falvo, J., Lu, K. S., Ciccarelli, R. B., and Holzschu, D. (1991) Effects of surface amino acid replacements in cytochrome c peroxidase on complex formation with cytochrome c, Biochemistry 30, 11585-11595.
    • (1991) Biochemistry , vol.30 , pp. 11585-11595
    • Corin, A.F.1    McLendon, G.2    Zhang, Q.3    Hake, R.A.4    Falvo, J.5    Lu, K.S.6    Ciccarelli, R.B.7    Holzschu, D.8
  • 22
    • 0027415476 scopus 로고
    • Effects of surface amino acid replacements in cytochrome c peroxidase on intracomplex electron transfer from cytochrome c
    • Corin, A. F., Hake, R. A., McLendon, G., Hazzard, J. T., and Tollin, T. (1993) Effects of surface amino acid replacements in cytochrome c peroxidase on intracomplex electron transfer from cytochrome c, Biochemistry 32, 2756-2762.
    • (1993) Biochemistry , vol.32 , pp. 2756-2762
    • Corin, A.F.1    Hake, R.A.2    McLendon, G.3    Hazzard, J.T.4    Tollin, T.5
  • 23
    • 0031042593 scopus 로고    scopus 로고
    • Photoinduced electron transfer between cytochrome c peroxidase (D37K) and Zn-substituted cytochrome c: Probing the two-domain binding and reactivity of the peroxidase
    • Zhou, J. S., Tran, S. T., McLendon, G., and Hoffman, B. M. (1997) Photoinduced electron transfer between cytochrome c peroxidase (D37K) and Zn-substituted cytochrome c: Probing the two-domain binding and reactivity of the peroxidase, J. Am. Chem. Soc. 119, 269-277.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 269-277
    • Zhou, J.S.1    Tran, S.T.2    McLendon, G.3    Hoffman, B.M.4
  • 24
    • 0034702763 scopus 로고    scopus 로고
    • Cytochrome c peroxidase-cytochrome c complex: Locating the second binding domain on cytochrome c peroxidase with site-directed mutagenesis
    • Leesch, V. W., Bujons, J., Mauk, A. G., and Hoffman, B. M. (2000) Cytochrome c peroxidase-cytochrome c complex: Locating the second binding domain on cytochrome c peroxidase with site-directed mutagenesis, Biochemistry 39, 10132-10139.
    • (2000) Biochemistry , vol.39 , pp. 10132-10139
    • Leesch, V.W.1    Bujons, J.2    Mauk, A.G.3    Hoffman, B.M.4
  • 25
    • 0029751080 scopus 로고    scopus 로고
    • A complete mechanism for steady-state oxidation of yeast cytochrome c by cytochrome c peroxidase
    • Miller, M. A. (1996) A complete mechanism for steady-state oxidation of yeast cytochrome c by cytochrome c peroxidase, Biochemistry 35, 15791-15799.
    • (1996) Biochemistry , vol.35 , pp. 15791-15799
    • Miller, M.A.1
  • 26
    • 0030959506 scopus 로고    scopus 로고
    • Cytochrome c/cytochrome c peroxidase complex: Effect of binding-site mutations on the thermodynamics of complex formation
    • Erman, J. E., Kresheck, G. K., Vitello, L. B., and Miller, A. M. (1997) Cytochrome c/cytochrome c peroxidase complex: Effect of binding-site mutations on the thermodynamics of complex formation, Biochemistry 36, 4054-4060.
    • (1997) Biochemistry , vol.36 , pp. 4054-4060
    • Erman, J.E.1    Kresheck, G.K.2    Vitello, L.B.3    Miller, A.M.4
  • 27
    • 0035895344 scopus 로고    scopus 로고
    • Interactions between yeast iso-1-cytochrome c and its peroxidase
    • Pielak, G. J., and Wang, X. (2001) Interactions between yeast iso-1-cytochrome c and its peroxidase, Biochemistry 40, 422-428.
    • (2001) Biochemistry , vol.40 , pp. 422-428
    • Pielak, G.J.1    Wang, X.2
  • 28
    • 1942469438 scopus 로고    scopus 로고
    • Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link
    • Guo, M., Bhaskar, B., Huiying, L., Barrows, T. P., and Poulos, T. L. (2004) Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link, Proc. Natl. Acad. Sci. U.S.A. 101, 5940-5945.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 5940-5945
    • Guo, M.1    Bhaskar, B.2    Huiying, L.3    Barrows, T.P.4    Poulos, T.L.5
  • 29
    • 33747454273 scopus 로고    scopus 로고
    • Characterization of a covalently-linked yeast cytochrome c/cytochrome c peroxidase complex: Evidence for a single, catalytically-active cytochrome c binding site on cytochrome c peroxidase
    • Nakani, S., Viriyakul, T., Mitchell, R., Vitello, L. B., and Erman, J. E. (2006) Characterization of a covalently-linked yeast cytochrome c/cytochrome c peroxidase complex: Evidence for a single, catalytically-active cytochrome c binding site on cytochrome c peroxidase, Biochemistry 45, 9887-9893.
    • (2006) Biochemistry , vol.45 , pp. 9887-9893
    • Nakani, S.1    Viriyakul, T.2    Mitchell, R.3    Vitello, L.B.4    Erman, J.E.5
  • 30
    • 33845244096 scopus 로고    scopus 로고
    • Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules
    • Nakani, S., Vitello, L. B., and Erman, J. E. (2006) Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules, Biochemistry 45, 14371-14378.
    • (2006) Biochemistry , vol.45 , pp. 14371-14378
    • Nakani, S.1    Vitello, L.B.2    Erman, J.E.3
  • 31
    • 34250838027 scopus 로고    scopus 로고
    • Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR
    • Volkov, A. N., Worrall, J. A. R., Holtzmann, E., and Ubbink, M. (2006) Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR, Proc. Natl. Acad. Sci. U.S.A. 103, 18945-18950.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18945-18950
    • Volkov, A.N.1    Worrall, J.A.R.2    Holtzmann, E.3    Ubbink, M.4
  • 32
    • 0029147018 scopus 로고
    • Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters
    • Matthis, A. L., and Erman, J. E. (1995) Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters, Biochemistry 34, 9991-9999.
    • (1995) Biochemistry , vol.34 , pp. 9991-9999
    • Matthis, A.L.1    Erman, J.E.2
  • 33
    • 0035834055 scopus 로고    scopus 로고
    • Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase
    • Savenkova, M. I., Satterlee, J. D., Erman, J. E., Siems, W. F., and Helms, G. L. (2001) Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase, Biochemistry 40, 12123-12131.
    • (2001) Biochemistry , vol.40 , pp. 12123-12131
    • Savenkova, M.I.1    Satterlee, J.D.2    Erman, J.E.3    Siems, W.F.4    Helms, G.L.5
  • 34
    • 0019170291 scopus 로고
    • Primary structure of yeast cytochrome c peroxidase II. The complete amino acid sequence
    • Takio, K., Titani, K., Ericsson, L. H., and Yonetani, T. (1980) Primary structure of yeast cytochrome c peroxidase II. The complete amino acid sequence, Arch. Biochem. Biophys. 203, 615-629.
    • (1980) Arch. Biochem. Biophys , vol.203 , pp. 615-629
    • Takio, K.1    Titani, K.2    Ericsson, L.H.3    Yonetani, T.4
  • 35
    • 0034130258 scopus 로고    scopus 로고
    • Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly purified holoenzymes
    • Teske, J. G., Savenkova, M. I., Mauro, J. M., Erman, J. E., and Satterlee, J. D. (2000) Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly purified holoenzymes, Protein Expression Purif. 19, 139-147.
    • (2000) Protein Expression Purif , vol.19 , pp. 139-147
    • Teske, J.G.1    Savenkova, M.I.2    Mauro, J.M.3    Erman, J.E.4    Satterlee, J.D.5
  • 37
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock, W. B. R., Rosell, F. I., Twitchett, M. B., Dumont, M. E., and Mauk, A. G. (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition, Biochemistry 37, 6124-6131.
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.R.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 38
    • 0023106193 scopus 로고
    • Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I
    • Fishel, L. A., Villafranca, J. E., Mauro, J. M., and Kraut, J. (1987) Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I, Biochemistry 26, 351-360.
    • (1987) Biochemistry , vol.26 , pp. 351-360
    • Fishel, L.A.1    Villafranca, J.E.2    Mauro, J.M.3    Kraut, J.4
  • 39
    • 0025359972 scopus 로고
    • pH-dependent spectral and kinetic properties of cytochrome c peroxidase: Comparison of freshly isolated and stored enzyme
    • Vitello, L. B., Huang, M., and Erman, J. E. (1990) pH-dependent spectral and kinetic properties of cytochrome c peroxidase: Comparison of freshly isolated and stored enzyme, Biochemistry 29, 4283-4288.
    • (1990) Biochemistry , vol.29 , pp. 4283-4288
    • Vitello, L.B.1    Huang, M.2    Erman, J.E.3
  • 40
    • 2142673905 scopus 로고
    • Hydrogen peroxide
    • Interscience, New York
    • Kolthoff, I. M., and Belcher, R. (1957) Hydrogen peroxide, in Volumetric Analysis, Vol. 3, pp 75-76, Interscience, New York.
    • (1957) Volumetric Analysis , vol.3 , pp. 75-76
    • Kolthoff, I.M.1    Belcher, R.2
  • 41
    • 0016693267 scopus 로고
    • A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength
    • Loo, S., and Erman, J. E. (1975) A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength, Biochemistry 14, 3467-3470.
    • (1975) Biochemistry , vol.14 , pp. 3467-3470
    • Loo, S.1    Erman, J.E.2
  • 42
    • 0026454818 scopus 로고
    • Effect of Asp-235 → Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase
    • Vitello, L. B., Erman, J. E., Miller, M. A., Mauro, J. M., and Kraut, J. (1992) Effect of Asp-235 → Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase, Biochemistry 31, 11524-11535.
    • (1992) Biochemistry , vol.31 , pp. 11524-11535
    • Vitello, L.B.1    Erman, J.E.2    Miller, M.A.3    Mauro, J.M.4    Kraut, J.5
  • 43
    • 0024298587 scopus 로고
    • Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c
    • Miller, M. A., Hazzard, J. T., Mauro, J. M., Edwards, S. L., Simons, P. C., Tollin, G., and Kraut, J. (1988) Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c, Biochemistry 27, 9081-9088.
    • (1988) Biochemistry , vol.27 , pp. 9081-9088
    • Miller, M.A.1    Hazzard, J.T.2    Mauro, J.M.3    Edwards, S.L.4    Simons, P.C.5    Tollin, G.6    Kraut, J.7
  • 44
    • 0025240820 scopus 로고
    • Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants
    • Vitello, L. B., Erman, J. E., Mauro, J. M., and Kraut, J. (1990) Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants, Biochim. Biophys. Acta 1038, 90-97.
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 90-97
    • Vitello, L.B.1    Erman, J.E.2    Mauro, J.M.3    Kraut, J.4
  • 45
    • 0029030445 scopus 로고
    • Site-specific cross-linking as a method for studying intramolecular electron transfer
    • Pappa, H. S., and Poulos, T. L. (1995) Site-specific cross-linking as a method for studying intramolecular electron transfer, Biochemistry 34, 6573-6580.
    • (1995) Biochemistry , vol.34 , pp. 6573-6580
    • Pappa, H.S.1    Poulos, T.L.2
  • 46
    • 0029865348 scopus 로고    scopus 로고
    • Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-linking
    • Pappa, H. S., Tajbaksh, S., Saunders, A. J., Pielak, G. J., and Poulos, T. L. (1996) Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-linking, Biochemistry 35, 4837-4845.
    • (1996) Biochemistry , vol.35 , pp. 4837-4845
    • Pappa, H.S.1    Tajbaksh, S.2    Saunders, A.J.3    Pielak, G.J.4    Poulos, T.L.5
  • 47
    • 4444242006 scopus 로고    scopus 로고
    • Electron transfer between cytochrome c and cytochrome c peroxidase in single crystals
    • Kang, S. A., Marjavaara, P. J., and Crane, B. R. (2004) Electron transfer between cytochrome c and cytochrome c peroxidase in single crystals, J. Am. Chem. Soc. 126, 10836-10837.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 10836-10837
    • Kang, S.A.1    Marjavaara, P.J.2    Crane, B.R.3
  • 48
    • 27344432508 scopus 로고    scopus 로고
    • Effects of interface mutations on association modes and electron-transfer rates between protein
    • Kang, S. A., and Crane, B. R. (2005) Effects of interface mutations on association modes and electron-transfer rates between protein, Proc. Natl. Acad. Sci. U.S.A. 102, 15465-15470.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 15465-15470
    • Kang, S.A.1    Crane, B.R.2
  • 49
    • 33644517862 scopus 로고    scopus 로고
    • Solvent isotope effects on interfacial protein electron transfer in crystals and electrode films
    • Kang, S. A., Hoke, K. R., and Crane, B. R. (2006) Solvent isotope effects on interfacial protein electron transfer in crystals and electrode films, J. Am. Chem. Soc. 128, 2346-2355.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 2346-2355
    • Kang, S.A.1    Hoke, K.R.2    Crane, B.R.3
  • 50
    • 0022418566 scopus 로고
    • A kinetic study of the alkaline transitions in cytochrome c peroxidase
    • Dhaliwal, B. K., and Erman, J. E. (1985) A kinetic study of the alkaline transitions in cytochrome c peroxidase, Biochim. Biophys. Acta 827, 174-182.
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 174-182
    • Dhaliwal, B.K.1    Erman, J.E.2


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