메뉴 건너뛰기




Volumn 31, Issue 4, 1998, Pages 307-327

Cytochrome c peroxidase: A model heme protein

Author keywords

Cytochrome c peroxidase; Hydrogen peroxide activation; Long range electron transfer; Protein protein interactions; Site directed mutagenesis

Indexed keywords


EID: 0032372059     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (35)

References (121)
  • 2
    • 0030597287 scopus 로고    scopus 로고
    • A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum
    • Aono, S., Nakajima, H., Saito, K. and Okada, M. (1996) A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum. Biochem. Biophys. Res. Commun. 228, 752-756.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 752-756
    • Aono, S.1    Nakajima, H.2    Saito, K.3    Okada, M.4
  • 3
    • 0023275184 scopus 로고
    • Thermodynamics of the two step formation of horseradish peroxidase compound I
    • Balny, C., Travers, F., Barman, T. and Douzou, P. (1987) Thermodynamics of the two step formation of horseradish peroxidase compound I. Eur. Biophys. J. 14, 375-383.
    • (1987) Eur. Biophys. J. , vol.14 , pp. 375-383
    • Balny, C.1    Travers, F.2    Barman, T.3    Douzou, P.4
  • 4
    • 0019876897 scopus 로고
    • Binding of arylazidocytochrome c to yeast cytochrome c peroxidase
    • Bisson, R. and Capaldi, R. A. (1981) Binding of arylazidocytochrome c to yeast cytochrome c peroxidase. J. Biol. Chem. 256, 4362-4367.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4362-4367
    • Bisson, R.1    Capaldi, R.A.2
  • 5
    • 0000170196 scopus 로고
    • Yeast cytochrome c peroxidase
    • Everse, J., Everse, K. E. and Grisham, M. B. (eds.), CRC Press, Boca Raton, Florida
    • Bosshard, H. R., Anni, H. and Yonetani, T. (1991) Yeast cytochrome c peroxidase; in Peroxidases in Chemistry and Biology, Vol. I, Everse, J., Everse, K. E. and Grisham, M. B. (eds.), pp. 51-84, CRC Press, Boca Raton, Florida.
    • (1991) Peroxidases in Chemistry and Biology , vol.1 , pp. 51-84
    • Bosshard, H.R.1    Anni, H.2    Yonetani, T.3
  • 6
    • 0022548334 scopus 로고
    • The pH dependence of the mechanism of reaction of hydrogen peroxide with a nonaggregating, non-μ-oxo dimer-forming iron(III) porphyrin in water
    • Bruice, T. C., Zipplies, M. F. and Lee, W. A. (1986) The pH dependence of the mechanism of reaction of hydrogen peroxide with a nonaggregating, non-μ-oxo dimer-forming iron(III) porphyrin in water. Proc. Natl. Acad. Sci. USA 83, 4646-4649.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4646-4649
    • Bruice, T.C.1    Zipplies, M.F.2    Lee, W.A.3
  • 7
    • 0015242098 scopus 로고
    • Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin
    • Brunori, M., Saggese, U., Rotilio, G. C., Antonini, E. and Wyman, J. (1971) Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin. Biochemistry 10, 1604-1609.
    • (1971) Biochemistry , vol.10 , pp. 1604-1609
    • Brunori, M.1    Saggese, U.2    Rotilio, G.C.3    Antonini, E.4    Wyman, J.5
  • 9
    • 0009499579 scopus 로고
    • Temperature dependence of the unimolecular reduction of ferricytochrome c by ferrocytochrome c peroxidase at low and high ionic strengths
    • Cheung, E. and English, A. M. (1988) Temperature dependence of the unimolecular reduction of ferricytochrome c by ferrocytochrome c peroxidase at low and high ionic strengths. Inorg. Chem. 27, 1078-1081.
    • (1988) Inorg. Chem. , vol.27 , pp. 1078-1081
    • Cheung, E.1    English, A.M.2
  • 10
    • 0018273821 scopus 로고
    • Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme
    • Conroy, C. W., Tyma, P., Daum, P. H. and Erman, J. E. (1978) Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme. Biochim. Biophys. Acta 537, 62-69.
    • (1978) Biochim. Biophys. Acta , vol.537 , pp. 62-69
    • Conroy, C.W.1    Tyma, P.2    Daum, P.H.3    Erman, J.E.4
  • 11
    • 0026340012 scopus 로고
    • Effects of surface amino acid replacement 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 Holzchu, D. (1991) Effects of surface amino acid replacement 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    Holzchu, D.8
  • 12
    • 0015239159 scopus 로고
    • Studies on cytochrome c peroxidase. XVII. Stoichiometry and mechanism of the reaction of compound ES with donors
    • Coulson, A. F. W., Erman, J. E. and Yonetani, T. (1971) Studies on cytochrome c peroxidase. XVII. Stoichiometry and mechanism of the reaction of compound ES with donors. J. Biol. Chem. 246, 917-924.
    • (1971) J. Biol. Chem. , vol.246 , pp. 917-924
    • Coulson, A.F.W.1    Erman, J.E.2    Yonetani, T.3
  • 13
    • 0024279606 scopus 로고
    • Replacement of lysine 32 in yeast cytochrome c: Effects on the binding and reactivity with physiological partners
    • Das, G., Hickey, D. R., Principio, L., Conklin, K. T., Short, J., Miller, J. R., McLendon, G. and Sherman, F. (1988) Replacement of lysine 32 in yeast cytochrome c: effects on the binding and reactivity with physiological partners. J. Biol. Chem. 263, 18290-18297.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18290-18297
    • Das, G.1    Hickey, D.R.2    Principio, L.3    Conklin, K.T.4    Short, J.5    Miller, J.R.6    McLendon, G.7    Sherman, F.8
  • 14
    • 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
  • 16
    • 0021471325 scopus 로고
    • Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase
    • Dowe, R. J., Vitello, L. B. and Erman, J. E. (1984) Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase. Arch. Biochem. Biophys. 232, 566-573.
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 566-573
    • Dowe, R.J.1    Vitello, L.B.2    Erman, J.E.3
  • 17
    • 0014038180 scopus 로고
    • Cytochrome c peroxidase. I. Preparation of the crystalline enzyme from baker's yeast
    • Ellfolk, N. (1967) Cytochrome c peroxidase. I. Preparation of the crystalline enzyme from baker's yeast. Acta Chem. Scand. 21, 175-181.
    • (1967) Acta Chem. Scand. , vol.21 , pp. 175-181
    • Ellfolk, N.1
  • 18
    • 0014619579 scopus 로고
    • Cytochrome c peroxidase. IV. Isoelectric focusing and analysis of the crystalline enzyme in an acidic pH gradient
    • Ellfolk, N. and Sievers, S. (1969) Cytochrome c peroxidase. IV. Isoelectric focusing and analysis of the crystalline enzyme in an acidic pH gradient. Acta Chem. Scand. 23, 2550-2551.
    • (1969) Acta Chem. Scand. , vol.23 , pp. 2550-2551
    • Ellfolk, N.1    Sievers, S.2
  • 19
    • 0003166132 scopus 로고
    • Reduction of ferrocytochrome c peroxidase. 4. Kinetics of yeast cytochrome c reduction at high buffer phosphate concentration
    • English, A. M. and Cheung, E. (1992) Reduction of ferrocytochrome c peroxidase. 4. Kinetics of yeast cytochrome c reduction at high buffer phosphate concentration. Inorganica Chemica Acta 201, 243-246.
    • (1992) Inorganica Chemica Acta , vol.201 , pp. 243-246
    • English, A.M.1    Cheung, E.2
  • 20
    • 0015971160 scopus 로고
    • Kinetic studies of fluoride binding by cytochrome c peroxidase
    • Erman, J. E. (1974a) Kinetic studies of fluoride binding by cytochrome c peroxidase. Biochemistry 13, 34-39.
    • (1974) Biochemistry , vol.13 , pp. 34-39
    • Erman, J.E.1
  • 21
    • 0015979118 scopus 로고
    • Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase
    • Erman, J. E. (1974b) Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase. Biochemistry 13, 39-44.
    • (1974) Biochemistry , vol.13 , pp. 39-44
    • Erman, J.E.1
  • 22
    • 0003186257 scopus 로고
    • The cytochrome c peroxidase oxidation of ferrocytochrome c: New insights into electron transfer complex formation and the catalytic mechanism from dynamic NMR studies
    • Erman, J. E. and Satterlee, J. D. (1995) The cytochrome c peroxidase oxidation of ferrocytochrome c: new insights into electron transfer complex formation and the catalytic mechanism from dynamic NMR studies. Adv. Biophys. Chem. 5, 141-178.
    • (1995) Adv. Biophys. Chem. , vol.5 , pp. 141-178
    • Erman, J.E.1    Satterlee, J.D.2
  • 23
    • 0019321339 scopus 로고
    • The binding of cytochrome c peroxidase and ferricytochrome c: A spectrophotometric determination of the equilibrium association constant as a function of ionic strength
    • Erman, J. E. and Vitello, L. B. (1980) The binding of cytochrome c peroxidase and ferricytochrome c: a spectrophotometric determination of the equilibrium association constant as a function of ionic strength. J. Biol. Chem. 255, 6224-6227.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6224-6227
    • Erman, J.E.1    Vitello, L.B.2
  • 24
    • 0016690880 scopus 로고
    • The oxidation of cytochrome c peroxidase by hydrogen peroxide: Characterization of products
    • Erman, J. E. and Yonetani, T. (1975a) The oxidation of cytochrome c peroxidase by hydrogen peroxide: characterization of products. Biochim. Biophys. Acta 393, 343-349.
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 343-349
    • Erman, J.E.1    Yonetani, T.2
  • 25
    • 0016833424 scopus 로고
    • A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound I
    • Erman, J. E. and Yonetani, T. (1975b) A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound I. Biochim. Biophys. Acta 393, 350-357.
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 350-357
    • Erman, J.E.1    Yonetani, T.2
  • 26
    • 0023644332 scopus 로고
    • A covalent complex between horse heart cytochrome c and yeast cytochrome c peroxidase: Kinetic properties
    • Erman, J. E., Kim, K. L., Vitello, L. B., Moench, S. J. and Satterlee, J. D. (1986) A covalent complex between horse heart cytochrome c and yeast cytochrome c peroxidase: kinetic properties. Biochim. Biophys. Acta 911, 1-10.
    • (1986) Biochim. Biophys. Acta , vol.911 , pp. 1-10
    • Erman, J.E.1    Kim, K.L.2    Vitello, L.B.3    Moench, S.J.4    Satterlee, J.D.5
  • 27
    • 0024430072 scopus 로고
    • Detection of an oxy-ferryl porphyrin π-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I
    • Erman, J. E., Vitello, L. B., Mauro, J. M. and Kraut, J. (1989) Detection of an oxy-ferryl porphyrin π-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I. Biochemistry 28, 7992-7995.
    • (1989) Biochemistry , vol.28 , pp. 7992-7995
    • Erman, J.E.1    Vitello, L.B.2    Mauro, J.M.3    Kraut, J.4
  • 28
    • 0000817524 scopus 로고
    • Electron transfer within the cytochrome c-cytochrome c peroxidase complex: Dependence of the transient-state and steady-state kinetics on ionic strength
    • Erman, J. E., Kang, D. S., Kim, K. L., Summers, F. E., Matthis, A. L. and Vitello, L. B. (1991) Electron transfer within the cytochrome c-cytochrome c peroxidase complex: dependence of the transient-state and steady-state kinetics on ionic strength. Mol. Cryst. Liq. Cryst. 194, 253-258.
    • (1991) Mol. Cryst. Liq. Cryst. , vol.194 , pp. 253-258
    • Erman, J.E.1    Kang, D.S.2    Kim, K.L.3    Summers, F.E.4    Matthis, A.L.5    Vitello, L.B.6
  • 29
    • 0000313831 scopus 로고
    • Active-site mutations in cytochrome c peroxidase: A critical role for histidine-52 in the rate of formation of compound I
    • Erman, J. E., Vitello, L. B., Miller, M. A. and Kraut, J. (1992) Active-site mutations in cytochrome c peroxidase: A critical role for histidine-52 in the rate of formation of compound I. J. Am. Chem. Soc. 114, 6592-6593.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6592-6593
    • Erman, J.E.1    Vitello, L.B.2    Miller, M.A.3    Kraut, J.4
  • 30
    • 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., Browne, 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    Browne, K.A.5    Kraut, J.6
  • 31
    • 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. C., Vitello, L. B. and Miller, M. A. (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.C.2    Vitello, L.B.3    Miller, M.A.4
  • 32
    • 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
  • 33
    • 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
  • 34
    • 0027994390 scopus 로고
    • Circular dichroism studies of the binding of mammalian and non-mammalian cytochromes c to cytochrome c oxidase, cytochrome c peroxidase, and polyanions
    • Garber, E. A. E. and Margoliash, E. (1994) Circular dichroism studies of the binding of mammalian and non-mammalian cytochromes c to cytochrome c oxidase, cytochrome c peroxidase, and polyanions. Biochim. Biophys. Acta 1187, 289-295.
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 289-295
    • Garber, E.A.E.1    Margoliash, E.2
  • 35
    • 0007792482 scopus 로고
    • A kinetic study of the reaction between ferrimyoglobin and hydrogen peroxide
    • George, P. and Irvine, D. H. (1956) A kinetic study of the reaction between ferrimyoglobin and hydrogen peroxide. J. Colloid Sci. 11, 327-339.
    • (1956) J. Colloid Sci. , vol.11 , pp. 327-339
    • George, P.1    Irvine, D.H.2
  • 36
    • 0026074926 scopus 로고
    • Photoinduced electron transfer between cytochrome c peroxidase and yeast cytochrome c labeled at cys 102 with (4-bromomethyl-4′-methylbipyridine)[bis(bipyridine)]ruthenium
    • Geren, L., Hahm, S., Durham, B. and Millet, F. (1991) Photoinduced electron transfer between cytochrome c peroxidase and yeast cytochrome c labeled at cys 102 with (4-bromomethyl-4′-methylbipyridine)[bis(bipyridine)]ruthenium. Biochemistry 30, 9450-9457.
    • (1991) Biochemistry , vol.30 , pp. 9450-9457
    • Geren, L.1    Hahm, S.2    Durham, B.3    Millet, F.4
  • 37
    • 33748392625 scopus 로고
    • Free radical produced in the reaction of metmyoglobin and hydrogen peroxide
    • Gibson, J. F., Ingram, D. J. E. and Nicholls, P. (1958) Free radical produced in the reaction of metmyoglobin and hydrogen peroxide. Nature (London) 181, 1398-1399.
    • (1958) Nature (London) , vol.181 , pp. 1398-1399
    • Gibson, J.F.1    Ingram, D.J.E.2    Nicholls, P.3
  • 38
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • Gilles-Gonzalez, M. A., Gonzalez, G. and Perutz, M. (1994) Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 33, 8097-8073.
    • (1994) Biochemistry , vol.33 , pp. 8097-18073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.3
  • 39
    • 0027231963 scopus 로고
    • The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme
    • Goodin, D. B. and McRee, D. E. (1993) The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry 32, 3313-3324.
    • (1993) Biochemistry , vol.32 , pp. 3313-3324
    • Goodin, D.B.1    McRee, D.E.2
  • 40
    • 1642503542 scopus 로고
    • Studies of the. radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis
    • Goodin, D. B., Mauk, A. G. and Smith, M. (1986) Studies of the. radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 83, 1295-1299.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1295-1299
    • Goodin, D.B.1    Mauk, A.G.2    Smith, M.3
  • 41
    • 0023645021 scopus 로고
    • The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51
    • Goodin, D. B., Mauk, A. G. and Smith, M. (1987) The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51. J. Biol. Chem. 262, 7719-7724.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7719-7724
    • Goodin, D.B.1    Mauk, A.G.2    Smith, M.3
  • 42
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • Gunther, M. R., Kelman, D. J., Corbett, J. T. and Mason, R. P. (1995) Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. J. Biol. Chem. 270, 16075-16081.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16075-16081
    • Gunther, M.R.1    Kelman, D.J.2    Corbett, J.T.3    Mason, R.P.4
  • 43
    • 0015932599 scopus 로고
    • Nuclear magnetic resonance study of the interaction of cytochrome c with cytochrome c peroxidase
    • Gupta, R. K. and Yonetani, T. (1973) Nuclear magnetic resonance study of the interaction of cytochrome c with cytochrome c peroxidase. Biochim. Biophys. Acta 292, 502-508.
    • (1973) Biochim. Biophys. Acta , vol.292 , pp. 502-508
    • Gupta, R.K.1    Yonetani, T.2
  • 44
    • 0026511735 scopus 로고
    • Photoinduced electron transfer between cytochrome c peroxidase and horse cytochrome c labeled at specific lysines with (dicarboxybipyridine)(bisbipyridine)ruthenium(II)
    • Hahm, S., Durham, B. and Millett, F. (1992) Photoinduced electron transfer between cytochrome c peroxidase and horse cytochrome c labeled at specific lysines with (dicarboxybipyridine)(bisbipyridine)ruthenium(II). Biochemistry 31, 3472-3477.
    • (1992) Biochemistry , vol.31 , pp. 3472-3477
    • Hahm, S.1    Durham, B.2    Millett, F.3
  • 45
    • 0000925694 scopus 로고
    • Reaction of cytochrome c with the radical in cytochrome c peroxidase compound I
    • Hahm, S., Geren, L., Durham, B. and Millett, F. (1993) Reaction of cytochrome c with the radical in cytochrome c peroxidase compound I. J. Am. Chem. Soc. 115, 3372-3373.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3372-3373
    • Hahm, S.1    Geren, L.2    Durham, B.3    Millett, F.4
  • 46
    • 0028209105 scopus 로고
    • Reaction of horse cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase I
    • Hahm, S., Miller, M. A., Geren, L., Kraut, J., Durham, B. and Millett, F. (1994) Reaction of horse cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase I. Biochemistry 33, 1473-1480.
    • (1994) Biochemistry , vol.33 , pp. 1473-1480
    • Hahm, S.1    Miller, M.A.2    Geren, L.3    Kraut, J.4    Durham, B.5    Millett, F.6
  • 47
    • 0000881549 scopus 로고
    • Redox-dependent molecular recognition in proteins: Site-directed mutagenesis suggests that cytochrome c oxidation state governs binding and recognition to cytochrome c peroxidase
    • Hake, R., McLendon, G., Conn, A. and Holzschu D. L. (1992) Redox-dependent molecular recognition in proteins: site-directed mutagenesis suggests that cytochrome c oxidation state governs binding and recognition to cytochrome c peroxidase. J. Am. Chem. Soc. 114, 5442-5443.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5442-5443
    • Hake, R.1    McLendon, G.2    Conn, A.3    Holzschu, D.L.4
  • 48
    • 0030725141 scopus 로고    scopus 로고
    • Extragenic compensation in complex formation: Restoration of binding of a charge reversal mutant of cytochrome c peroxidase(D217K) by a compensatory charge reversal in cytochrome c(K77D)
    • Hake, R., Corin, A. and McLendon, G. (1997) Extragenic compensation in complex formation: restoration of binding of a charge reversal mutant of cytochrome c peroxidase(D217K) by a compensatory charge reversal in cytochrome c(K77D). J. Am. Chem. Soc. 119, 10557-10558.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10557-10558
    • Hake, R.1    Corin, A.2    McLendon, G.3
  • 49
    • 0023659397 scopus 로고
    • Kinetics of reduction by free flavin semiquinones of the components of the cytochrome c-cytochrome c peroxidase complex and intracomplex electron transfer
    • Hazzard, J. T., Poulos, T. L. and Tollin G. (1987) Kinetics of reduction by free flavin semiquinones of the components of the cytochrome c-cytochrome c peroxidase complex and intracomplex electron transfer. Biochemistry 26, 2836-2848.
    • (1987) Biochemistry , vol.26 , pp. 2836-2848
    • Hazzard, J.T.1    Poulos, T.L.2    Tollin, G.3
  • 50
    • 0023915627 scopus 로고
    • Kinetics of intracomplex electron transfer and of reduction of the components of covalent and non-covalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinones
    • Hazzard, J. T., Moench, S. J., Erman, J. E., Satterlee, J. D. and Tollin, G. (1988) Kinetics of intracomplex electron transfer and of reduction of the components of covalent and non-covalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinones. Biochemistry 27, 2002-2008.
    • (1988) Biochemistry , vol.27 , pp. 2002-2008
    • Hazzard, J.T.1    Moench, S.J.2    Erman, J.E.3    Satterlee, J.D.4    Tollin, G.5
  • 51
    • 0026600906 scopus 로고
    • Cytochrome c and cytochrome c peroxidase complex as studied by resonance Raman spectroscopy
    • Hildebrandt, P., English, A. M. and Smulevich, G. (1992) Cytochrome c and cytochrome c peroxidase complex as studied by resonance Raman spectroscopy. Biochemistry 31, 2384-2392.
    • (1992) Biochemistry , vol.31 , pp. 2384-2392
    • Hildebrandt, P.1    English, A.M.2    Smulevich, G.3
  • 52
    • 0021772493 scopus 로고
    • Kinetics and energetics of intramolecular electron transfer in yeast cytochrome c peroxidase
    • Ho, P. S., Hoffman, B. M., Solomon, N., Kang, C. H. and Margoliash, E. (1984) Kinetics and energetics of intramolecular electron transfer in yeast cytochrome c peroxidase. Biochemistry 23, 4122-4128.
    • (1984) Biochemistry , vol.23 , pp. 4122-4128
    • Ho, P.S.1    Hoffman, B.M.2    Solomon, N.3    Kang, C.H.4    Margoliash, E.5
  • 53
    • 0001475069 scopus 로고
    • Species specificity of long-range electron transfer within the complex between zinc-substituted cytochrome c peroxidase and cytochrome c
    • Ho, P. S., Sutoris, C., Liang, N., Margoliash, E. and Hoffman, B. M. (1985) Species specificity of long-range electron transfer within the complex between zinc-substituted cytochrome c peroxidase and cytochrome c. J. Am. Chem. Soc. 107, 1070-1071.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1070-1071
    • Ho, P.S.1    Sutoris, C.2    Liang, N.3    Margoliash, E.4    Hoffman, B.M.5
  • 54
    • 0021765932 scopus 로고
    • Heme accessibility in the ferricytochrome c-cytochrome c peroxidase complex
    • Hoth, L. R. and Erman, J. E. (1984) Heme accessibility in the ferricytochrome c-cytochrome c peroxidase complex. Biochim. Biophys. Acta 788, 151-153.
    • (1984) Biochim. Biophys. Acta , vol.788 , pp. 151-153
    • Hoth, L.R.1    Erman, J.E.2
  • 55
    • 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
  • 56
    • 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
  • 58
    • 0025108493 scopus 로고
    • Cytochrome c peroxidase catalyzed oxidation of ferrocytochrome c by hydrogen peroxide: Ionic strength dependence of the steady-state rate parameters
    • Kim, K. L., Kang, D. S., Vitello, L. B. and Erman, J. E. (1990) Cytochrome c peroxidase catalyzed oxidation of ferrocytochrome c by hydrogen peroxide: ionic strength dependence of the steady-state rate parameters. Biochemistry 32, 9150-9159.
    • (1990) Biochemistry , vol.32 , pp. 9150-9159
    • Kim, K.L.1    Kang, D.S.2    Vitello, L.B.3    Erman, J.E.4
  • 59
    • 0023051676 scopus 로고
    • The binding of porphyrin cytochrome c to yeast cytochrome c peroxidase: A fluorescence study of the number of sites and their sensitivity to salt
    • Kornblatt, J. A. and English, A. M. (1986) The binding of porphyrin cytochrome c to yeast cytochrome c peroxidase: a fluorescence study of the number of sites and their sensitivity to salt. Eur. J. Biochem. 155, 505-511.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 505-511
    • Kornblatt, J.A.1    English, A.M.2
  • 60
    • 0029042647 scopus 로고
    • Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase
    • Kresheck, G. C., Vitello, L. B. and Erman, J. E. (1995) Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase. Biochemistry 34, 8398-8405.
    • (1995) Biochemistry , vol.34 , pp. 8398-8405
    • Kresheck, G.C.1    Vitello, L.B.2    Erman, J.E.3
  • 61
    • 0015972671 scopus 로고
    • Interaction of cytochrome c peroxidase with cytochrome c
    • Leonard, J. J. and Yonetani, T. (1974) Interaction of cytochrome c peroxidase with cytochrome c. Biochemistry 13, 1465-1468.
    • (1974) Biochemistry , vol.13 , pp. 1465-1468
    • Leonard, J.J.1    Yonetani, T.2
  • 62
    • 0000369891 scopus 로고
    • Long-range electron transfer from iron(II)-cytochrome c to (zinc-cytochrome c peroxidase)(+) within the 1:1 complex
    • Liang, N., Kang, C. H., Ho, P. S., Margoliash, E. and Hoffman, B. M. (1986) Long-range electron transfer from iron(II)-cytochrome c to (zinc-cytochrome c peroxidase)(+) within the 1:1 complex. J. Am. Chem. Soc. 108, 4665-4666.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 4665-4666
    • Liang, N.1    Kang, C.H.2    Ho, P.S.3    Margoliash, E.4    Hoffman, B.M.5
  • 63
    • 0024287523 scopus 로고
    • Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c
    • Liang, N., Mauk, A. G., Pielak, G. J., Johnson, J. A., Smith, M. and Hoffman, B. M. (1988) Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science 240, 311-313.
    • (1988) Science , vol.240 , pp. 311-313
    • Liang, N.1    Mauk, A.G.2    Pielak, G.J.3    Johnson, J.A.4    Smith, M.5    Hoffman, B.M.6
  • 64
    • 0028048863 scopus 로고
    • Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II
    • Liu, R. Q., Miller, M. A., Han, G. W., Hahm, S., Geren, L., Hibdon, S., Kraut, J., Durham, B. and Millett, F. (1994) Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II. Biochemistry 33, 8678-8685.
    • (1994) Biochemistry , vol.33 , pp. 8678-8685
    • Liu, R.Q.1    Miller, M.A.2    Han, G.W.3    Hahm, S.4    Geren, L.5    Hibdon, S.6    Kraut, J.7    Durham, B.8    Millett, F.9
  • 65
    • 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
  • 67
    • 0029126465 scopus 로고
    • Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength 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 of the steady-state parameters. Biochemistry 34, 9985-9990.
    • (1995) Biochemistry , vol.34 , pp. 9985-9990
    • Matthis, A.L.1    Erman, J.E.2
  • 68
    • 0029147018 scopus 로고
    • Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength
    • Matthis, A. L., Vitello, L. B. and Erman, J. E. (1995) Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength. Biochemistry 34, 9991-9999.
    • (1995) Biochemistry , vol.34 , pp. 9991-9999
    • Matthis, A.L.1    Vitello, L.B.2    Erman, J.E.3
  • 69
    • 0028062898 scopus 로고
    • Proton linkage in formation of the cytochrome c-cytochrome c peroxidase complex: Electrostatic properties of the high- and low-affinity cytochrome binding sites of the peroxidase
    • Mauk, K. 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 binding sites of the peroxidase. Biochemistry 33, 12609-12614.
    • (1994) Biochemistry , vol.33 , pp. 12609-12614
    • Mauk, K.R.1    Ferrer, J.C.2    Mauk, A.G.3
  • 70
    • 0345318403 scopus 로고
    • Long-distance electron transfer in proteins and model systems
    • McLendon, G. (1988) Long-distance electron transfer in proteins and model systems. Acc. Chem. Res. 21, 160-167.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 160-167
    • McLendon, G.1
  • 71
    • 0000412653 scopus 로고
    • Thermodynamic and kinetic aspects of binding and recognition in the cytochrome c/cytochrome c peroxidase complex
    • Mclendon, G., Zhang, Q., Wallin, S. A., Miller, R. M., Billstone, V., Spears, K. G. and Hoffman, B. M. (1993) Thermodynamic and kinetic aspects of binding and recognition in the cytochrome c/cytochrome c peroxidase complex. J. Am. Chem. Soc. 115, 3665-3669.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3665-3669
    • Mclendon, G.1    Zhang, Q.2    Wallin, S.A.3    Miller, R.M.4    Billstone, V.5    Spears, K.G.6    Hoffman, B.M.7
  • 72
    • 0029768641 scopus 로고    scopus 로고
    • Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site
    • Mei, H., Wang, K., McKee, S., Wang, X., Waldner, J. L., Pielak, G. J., Durham, B. and Millett F. (1996) Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site. Biochemistry 35, 15800-15806.
    • (1996) Biochemistry , vol.35 , pp. 15800-15806
    • Mei, H.1    Wang, K.2    McKee, S.3    Wang, X.4    Waldner, J.L.5    Pielak, G.J.6    Durham, B.7    Millett, F.8
  • 73
    • 0024788454 scopus 로고
    • Electron spin resonance spectrum of Tyr-151 free radical formed in reactions of sperm whale metmyoglobin with ethyl hydroperoxide and potassium iridate
    • Miki, H., Haada, K., Yamazaki, I., Tamira, M. and Watanabe, H. (1989) Electron spin resonance spectrum of Tyr-151 free radical formed in reactions of sperm whale metmyoglobin with ethyl hydroperoxide and potassium iridate. Arch. Biochem. Biophys. 275, 354-362.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 354-362
    • Miki, H.1    Haada, K.2    Yamazaki, I.3    Tamira, M.4    Watanabe, H.5
  • 74
    • 0029751080 scopus 로고    scopus 로고
    • A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase
    • Miller, M. A. (1996) A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase. Biochemistry 35, 15791-15799.
    • (1996) Biochemistry , vol.35 , pp. 15791-15799
    • Miller, M.A.1
  • 75
    • 0028065201 scopus 로고
    • Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I
    • Miller, M. A., Liu, R. Q., Hahm, S., Geren, L., Hibdon, S., Kraut, J., Durham, B. and Millett, F. (1994a) Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Biochemistry 33, 8686-8693.
    • (1994) Biochemistry , vol.33 , pp. 8686-8693
    • Miller, M.A.1    Liu, R.Q.2    Hahm, S.3    Geren, L.4    Hibdon, S.5    Kraut, J.6    Durham, B.7    Millett, F.8
  • 76
    • 0028076456 scopus 로고
    • 2.2 Å structure of oxy-peroxidase as a model for the transient enzyme:peroxide complex
    • Miller, M. A., Shaw, A. and Kraut, J. (1994b) 2.2 Å structure of oxy-peroxidase as a model for the transient enzyme:peroxide complex. Structural Biol. 1, 524-531.
    • (1994) Structural Biol. , vol.1 , pp. 524-531
    • Miller, M.A.1    Shaw, A.2    Kraut, J.3
  • 77
    • 0029126537 scopus 로고
    • Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase
    • Miller, M. A., Vitello, L. B. and Erman, J. E. (1995) Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase. Biochemistry 34, 12049-12058.
    • (1995) Biochemistry , vol.34 , pp. 12049-12058
    • Miller, M.A.1    Vitello, L.B.2    Erman, J.E.3
  • 78
    • 0014932623 scopus 로고
    • The nature of complex formation between cytochrome c and cytochrome c peroxidase
    • Mochan, E. (1970) The nature of complex formation between cytochrome c and cytochrome c peroxidase. Biochim. Biophys. Acta 216, 80-95.
    • (1970) Biochim. Biophys. Acta , vol.216 , pp. 80-95
    • Mochan, E.1
  • 79
    • 0014974138 scopus 로고
    • Complex-formation between cytochrome c and cytochrome c peroxidase: Equilibrium and titration studies
    • Mochan, E. and Nicholls, P. (1971) Complex-formation between cytochrome c and cytochrome c peroxidase: equilibrium and titration studies. Biochem. J. 121, 69-82.
    • (1971) Biochem. J. , vol.121 , pp. 69-82
    • Mochan, E.1    Nicholls, P.2
  • 80
    • 0023668285 scopus 로고
    • Proton NMR and electrophoretic studies of the covalent complex formed by crosslinking yeast cytochrome c peroxidase and horse cytochrome c with a water soluble carbodiimide
    • Moench, S. J., Satterlee, J. D. and Erman, J. E. (1987) Proton NMR and electrophoretic studies of the covalent complex formed by crosslinking yeast cytochrome c peroxidase and horse cytochrome c with a water soluble carbodiimide. Biochemistry 26, 3821-3826.
    • (1987) Biochemistry , vol.26 , pp. 3821-3826
    • Moench, S.J.1    Satterlee, J.D.2    Erman, J.E.3
  • 81
    • 0026652143 scopus 로고
    • Proton NMR comparison of noncovalent and covalently crosslinked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochrome c
    • Moench, S. J., Chroni, S., Lou, B.-S., Erman, J. E. and Satterlee, J. D. (1992) Proton NMR comparison of noncovalent and covalently crosslinked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochrome c. Biochemistry 31, 3661-3670.
    • (1992) Biochemistry , vol.31 , pp. 3661-3670
    • Moench, S.J.1    Chroni, S.2    Lou, B.-S.3    Erman, J.E.4    Satterlee, J.D.5
  • 82
    • 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., Priyadarshy, 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    Priyadarshy, S.4    Beratan, D.N.5    Onuchic, J.N.6    Hoffman, B.M.7
  • 83
    • 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
  • 84
    • 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
  • 85
    • 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
  • 86
    • 0021930234 scopus 로고
    • Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function
    • Pielak, G. J., Mauk, A. G. and Smith, M (1985) Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function. Nature 313, 152-154.
    • (1985) Nature , vol.313 , pp. 152-154
    • Pielak, G.J.1    Mauk, A.G.2    Smith, M.3
  • 87
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T. L. and Kraut, J. (1980a) 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
  • 88
    • 0019321862 scopus 로고
    • A hypothetical model of the cytochrome c peroxidase-cytochrome c electron transfer complex
    • Poulos, T. L. and Kraut, J. (1980b) 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
  • 89
    • 0017808971 scopus 로고
    • Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase
    • Poulos, T. L., Freer, S. T., Alden, R. A., Xuong, N., Edwards, S. L., Hamlin, R. C. and Kraut, J. (1978) Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase. J. Biol. Chem. 253, 3730-3735.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3730-3735
    • Poulos, T.L.1    Freer, S.T.2    Alden, R.A.3    Xuong, N.4    Edwards, S.L.5    Hamlin, R.C.6    Kraut, J.7
  • 91
    • 0023658734 scopus 로고
    • A proton NMR study of the non-covalent complex of horse cytochrome c and yeast cytochrome c peroxidase and its comparison with other interacting protein complexes
    • Satterlee, J. D., Moench, S. J. and Erman, J. E. (1987) A proton NMR study of the non-covalent complex of horse cytochrome c and yeast cytochrome c peroxidase and its comparison with other interacting protein complexes. Biochim. Biophys. Acta 912, 87-97.
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 87-97
    • Satterlee, J.D.1    Moench, S.J.2    Erman, J.E.3
  • 92
    • 85005470422 scopus 로고
    • Recent ENDOR and pulsed electron paramagnetic resonance studies of cytochrome c peroxidase-compound I and its site-directed mutants
    • Scholes, C. P., Liu, Y., Fishel, L. A., Farnum, M. F., Mauro, J. M. and Kraut, J. (1989) Recent ENDOR and pulsed electron paramagnetic resonance studies of cytochrome c peroxidase-compound I and its site-directed mutants. Israel J. Chem. 29, 85-92.
    • (1989) Israel J. Chem. , vol.29 , pp. 85-92
    • Scholes, C.P.1    Liu, Y.2    Fishel, L.A.3    Farnum, M.F.4    Mauro, J.M.5    Kraut, J.6
  • 94
    • 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
  • 95
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone, J. R. and Marietta, M. A. (1994) Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33, 5636-5640.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marietta, M.A.2
  • 96
    • 0023676224 scopus 로고
    • Reduction of cytochrome c peroxidase compounds I and II by ferrocytochrome c. A stopped-flow kinetic investigation
    • Summers, F. E. and Erman, J. E. (1988) Reduction of cytochrome c peroxidase compounds I and II by ferrocytochrome c. A stopped-flow kinetic investigation. J. Biol. Chem. 263, 14267-14275.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14267-14275
    • Summers, F.E.1    Erman, J.E.2
  • 97
    • 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
  • 98
    • 0014429072 scopus 로고
    • Kinetics of binding of, cyanide to sperm whale metmyoglobin
    • Ver Ploeg, D. A. and Alberty, R. A. (1968) Kinetics of binding of, cyanide to sperm whale metmyoglobin. J. Biol. Chem. 243, 435-440.
    • (1968) J. Biol. Chem. , vol.243 , pp. 435-440
    • Ver Ploeg, D.A.1    Alberty, R.A.2
  • 99
    • 0023442619 scopus 로고
    • Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: A fluorescence quenching study on the ionic strength dependence of the interaction
    • Vitello, L. B. and Erman, J. E. (1987) Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase: a fluorescence quenching study on the ionic strength dependence of the interaction. Arch. Biochem. Biophys. 258, 621-629.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 621-629
    • Vitello, L.B.1    Erman, J.E.2
  • 100
    • 0025240820 scopus 로고
    • Characterization of the hydrogen peroxide - Enzyme reaction for two cytochrome c mutants
    • Vitello, L. B., Erman, J. E., Mauro, J. M. and Kraut, J. (1990a) Characterization of the hydrogen peroxide - enzyme reaction for two cytochrome c 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
  • 101
    • 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. (1990b) 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
  • 102
    • 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
  • 103
    • 0027424783 scopus 로고
    • Effect of arginine-48 replacement and the reaction between cytochrome c peroxidase and hydrogen peroxide
    • Vitello, L. B., Erman, J. E., Miller, M. A., Wang, J. and Kraut, J. (1993) Effect of arginine-48 replacement and the reaction between cytochrome c peroxidase and hydrogen peroxide. Biochemistry 32, 9807-9818.
    • (1993) Biochemistry , vol.32 , pp. 9807-9818
    • Vitello, L.B.1    Erman, J.E.2    Miller, M.A.3    Wang, J.4    Kraut, J.5
  • 104
    • 0001489290 scopus 로고
    • Multiphasic intracomplex electron transfer from cytochrome c to Zn cytochrome c peroxidase: Conformational control of reactivity
    • Wallin, S. A., Stemp, E. D. A., Everest, A. M., Nocek, J. M., Netzel, T. L. and Hoffman, B. M. (1991) Multiphasic intracomplex electron transfer from cytochrome c to Zn cytochrome c peroxidase: conformational control of reactivity. J. Am. Chem. Soc. 113, 1842-1844.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1842-1844
    • Wallin, S.A.1    Stemp, E.D.A.2    Everest, A.M.3    Nocek, J.M.4    Netzel, T.L.5    Hoffman, B.M.6
  • 105
    • 0025334712 scopus 로고
    • X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis
    • Wang, J., Mauro, J. M., Edwards, S. L., Oatley, S. J., Fishel, L. A., Ashford, V. A., Xuong, N. and Kraut, J. (1990) X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis. Biochemistry 29, 7160-7173.
    • (1990) Biochemistry , vol.29 , pp. 7160-7173
    • Wang, J.1    Mauro, J.M.2    Edwards, S.L.3    Oatley, S.J.4    Fishel, L.A.5    Ashford, V.A.6    Xuong, N.7    Kraut, J.8
  • 106
    • 12644291216 scopus 로고    scopus 로고
    • Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase
    • Wang, K., Mei, H., Miller, M. A., Saunders, A., Wang, X., Waldner, J. L., Pielak, G. J., Durham, B. and Millett, F. (1996) Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase. Biochemistry 35, 15107-15119.
    • (1996) Biochemistry , vol.35 , pp. 15107-15119
    • Wang, K.1    Mei, H.2    Miller, M.A.3    Saunders, A.4    Wang, X.5    Waldner, J.L.6    Pielak, G.J.7    Durham, B.8    Millett, F.9
  • 107
    • 85022503788 scopus 로고
    • Ferricytochrome c binding induces detectable proton NMR shift changes in cytochrome c peroxidase-CN
    • Yi, Q., Erman, J. E. and Satterlee, J. D. (1992) Ferricytochrome c binding induces detectable proton NMR shift changes in cytochrome c peroxidase-CN. J. Am. Chem. Soc. 114, 7907-7909.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7907-7909
    • Yi, Q.1    Erman, J.E.2    Satterlee, J.D.3
  • 108
    • 0027487233 scopus 로고
    • Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c
    • Yi, Q., Erman, J. E. and Satterlee, J. D. (1993a) Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c. Biochemistry 32, 10988-10994.
    • (1993) Biochemistry , vol.32 , pp. 10988-10994
    • Yi, Q.1    Erman, J.E.2    Satterlee, J.D.3
  • 109
    • 21344489951 scopus 로고
    • Proton NMR study of a non-covalent complex formed between cytochrome c peroxidase-cyanide and tuna ferricytochrome c
    • Yi, Q., Satterlee, J. D. and Erman, J. E. (1993b) Proton NMR study of a non-covalent complex formed between cytochrome c peroxidase-cyanide and tuna ferricytochrome c. Mag. Reson. Chem. 31, S53-S58.
    • (1993) Mag. Reson. Chem. , vol.31
    • Yi, Q.1    Satterlee, J.D.2    Erman, J.E.3
  • 110
    • 0028121691 scopus 로고
    • 1H-NMR evaluation of yeast isozyme-1 ferricytochrome c equilibrium exchange dynamics in noncovalent complexes with two forms of yeast cytochrome c peroxidase
    • 1H-NMR evaluation of yeast isozyme-1 ferricytochrome c equilibrium exchange dynamics in noncovalent complexes with two forms of yeast cytochrome c peroxidase. J. Am. Chem. Soc. 116, 1981-1987.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1981-1987
    • Yi, Q.1    Erman, J.E.2    Satterlee, J.D.3
  • 111
    • 0027988442 scopus 로고
    • Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy
    • Yi, Q., Erman J. E. and Satterlee, J. D. (1994b) Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy. Biochemistry 33, 12032-12041.
    • (1994) Biochemistry , vol.33 , pp. 12032-12041
    • Yi, Q.1    Erman, J.E.2    Satterlee, J.D.3
  • 112
    • 0014199262 scopus 로고
    • Studies on cytochrome c peroxidase. X. Crystalline apo- and reconstituted holoenzymes
    • Yonetani, T. (1967) Studies on cytochrome c peroxidase. X. Crystalline apo- and reconstituted holoenzymes. J. Biol. Chem. 242, 5008-5013.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5008-5013
    • Yonetani, T.1
  • 113
    • 77956897161 scopus 로고
    • Cytochrome c peroxidase
    • 3rd Ed., Boyer, P. D. (ed.), Academic Press, New York
    • Yonetani, T. (1976) Cytochrome c peroxidase; in The Enzymes, Vol. 13, Part C, 3rd Ed., Boyer, P. D. (ed.), pp. 345-361, Academic Press, New York.
    • (1976) The Enzymes , vol.13 , Issue.PART C , pp. 345-361
    • Yonetani, T.1
  • 114
    • 0014010171 scopus 로고
    • Studies on cytochrome c peroxidase. III. Kinetics of the peroxidatic oxidation of ferrocytochrome c catalyzed by cytochrome c peroxidase
    • Yonetani, T. and Ray, G. S. (1966) Studies on cytochrome c peroxidase. III. Kinetics of the peroxidatic oxidation of ferrocytochrome c catalyzed by cytochrome c peroxidase. J. Biol. Chem. 241, 700-706.
    • (1966) J. Biol. Chem. , vol.241 , pp. 700-706
    • Yonetani, T.1    Ray, G.S.2
  • 115
    • 0014216604 scopus 로고
    • Studies on cytochrome c peroxidase. IX. The reaction of ferrimyoglobin with hydroperoxides and a comparison of peroxide-induced compounds of ferrimyoglobin and cytochrome c peroxidase
    • Yonetani, T. and Schleyer, H. (1967) Studies on cytochrome c peroxidase. IX. The reaction of ferrimyoglobin with hydroperoxides and a comparison of peroxide-induced compounds of ferrimyoglobin and cytochrome c peroxidase. J. Biol. Chem. 242, 1974-1979.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1974-1979
    • Yonetani, T.1    Schleyer, H.2
  • 116
    • 0014010869 scopus 로고
    • Studies on cytochrome c peroxidase. VII. Electron paramagnetic resonance absorptions of the enzyme and complex ES in dissolved and crystalline forms
    • Yonetani, T., Schleyer, H. and Ehrenberg, A. (1966) Studies on cytochrome c peroxidase. VII. Electron paramagnetic resonance absorptions of the enzyme and complex ES in dissolved and crystalline forms. J. Biol. Chem. 241, 3240-3242.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3240-3242
    • Yonetani, T.1    Schleyer, H.2    Ehrenberg, A.3
  • 117
    • 0000789855 scopus 로고
    • Influence of hydrogen ion activity and general acid-base catalysis on the rate of decomposition of hydrogen peroxide by a novel nonaggregating water-soluble iron(III) tetraphenylporphyrin derivative
    • Zipplies, M. F., Lee, W. A. and Bruice, T. C. (1986) Influence of hydrogen ion activity and general acid-base catalysis on the rate of decomposition of hydrogen peroxide by a novel nonaggregating water-soluble iron(III) tetraphenylporphyrin derivative. J. Am. Chem. Soc. 108, 4433-4445.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 4433-4445
    • Zipplies, M.F.1    Lee, W.A.2    Bruice, T.C.3
  • 118
    • 0001241132 scopus 로고
    • Cytochrome c peroxidase simultaneously binds cytochrome c at two different sites with strikingly different reactivities: Titrating a "substrate" with an enzyme
    • Zhou, J. S. and Hoffman, B. M. (1993) Cytochrome c peroxidase simultaneously binds cytochrome c at two different sites with strikingly different reactivities: titrating a "substrate" with an enzyme. J. Am. Chem. Soc. 115, 11008-11009.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11008-11009
    • Zhou, J.S.1    Hoffman, B.M.2
  • 119
    • 0028028129 scopus 로고
    • Stern-Volmer in reverse: 2:1 stoichiometry of the cytochrome c-cytochrome c peroxidase electron-transfer complex
    • Zhou, J. S. and Hoffman. B. M. (1994) Stern-Volmer in reverse: 2:1 stoichiometry of the cytochrome c-cytochrome c peroxidase electron-transfer complex. Science 265, 1693-1696.
    • (1994) Science , vol.265 , pp. 1693-1696
    • Zhou, J.S.1    Hoffman, B.M.2
  • 120
    • 0029643520 scopus 로고
    • Inhibitor-enhanced electron transfer: Copper cytochrome c as a redox-inert probe of ternary complexes
    • Zhou, J. S., Nocek, J. M., DeVan, M. L. and Hoffman, B. M. (1995) Inhibitor-enhanced electron transfer: copper cytochrome c as a redox-inert probe of ternary complexes. Science 269, 204-207.
    • (1995) Science , vol.269 , pp. 204-207
    • Zhou, J.S.1    Nocek, J.M.2    DeVan, M.L.3    Hoffman, B.M.4
  • 121
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.