메뉴 건너뛰기




Volumn 243, Issue 1-2, 1997, Pages 72-84

Charge reversal of a critical active-site residue of cytochrome-c peroxidase. Characterization of the Arg48→Glu variant

Author keywords

Compound 1; Cytochrome c peroxidase; EPR; Kinetics; NMR

Indexed keywords

CYTOCHROME C PEROXIDASE; RECOMBINANT ENZYME;

EID: 0031019879     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.72_1a.x     Document Type: Article
Times cited : (27)

References (67)
  • 1
    • 0000170196 scopus 로고
    • Yeast cytochrome c peroxidase
    • Everse, J., Everse, K. E. & Grisham, M. B., eds CRC Press, Boca Raton
    • Bosshard, H. R., Anni, H. & Yonetani, T. (1991) Yeast cytochrome c peroxidase, in Peroxidases in chemistry and biology (Everse, J., Everse, K. E. & Grisham, M. B., eds) vol. 2, pp. 52-78, CRC Press, Boca Raton.
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 52-78
    • Bosshard, H.R.1    Anni, H.2    Yonetani, T.3
  • 2
    • 0024545028 scopus 로고
    • Structural characterization of cytochrome c peroxidase by resonance Raman scattering
    • Dasgupta, S., Rousseau, D. L., Anni, H. & Yonetani, T. (1989) Structural characterization of cytochrome c peroxidase by resonance Raman scattering, J. Biol. Chem. 264, 654-662.
    • (1989) J. Biol. Chem. , vol.264 , pp. 654-662
    • Dasgupta, S.1    Rousseau, D.L.2    Anni, H.3    Yonetani, T.4
  • 3
    • 0023655398 scopus 로고
    • Yeast cytochrome c peroxidase. Coordination and spin states of heme prosthetic group
    • Yonetani, T. & Anni, H. (1987) Yeast cytochrome c peroxidase. Coordination and spin states of heme prosthetic group, J. Biol. Chem. 262, 9547-9554.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9547-9554
    • Yonetani, T.1    Anni, H.2
  • 4
    • 0024473758 scopus 로고
    • Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES
    • Sivaraja, M., Goodin, D. B., Smith, M. & Hoffman, B. M. (1989) Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES, Science 245, 738-740.
    • (1989) Science , vol.245 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 5
    • 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, F. M., Mauro, J. M. & Kraut, J. (1989) Recent ENDOR and pulsed electron paramagnetic resonance studies of cytochrome c peroxidase-compound I and its site-directed mutants, Isr. J. Chem. 29, 85-92.
    • (1989) Isr. J. Chem. , vol.29 , pp. 85-92
    • Scholes, C.P.1    Liu, Y.2    Fishel, L.A.3    Farnum, F.M.4    Mauro, J.M.5    Kraut, J.6
  • 6
    • 0025863971 scopus 로고
    • Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: Effects on coordination, species preference for cytochrome c, and electron transfer
    • Goodin, D. B., Davidson, M. G., Roe, J. A., Mauk, A. G. & Smith, M. (1991) Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer, Biochemistry 30, 4953-4962.
    • (1991) Biochemistry , vol.30 , pp. 4953-4962
    • Goodin, D.B.1    Davidson, M.G.2    Roe, J.A.3    Mauk, A.G.4    Smith, M.5
  • 7
    • 0027424783 scopus 로고
    • Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide
    • Vitello, L. B., Erman, J. E., Miller, M. A., Wang, J. & Kraut, J. (1993) Effect of arginine-48 replacement on 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
  • 8
    • 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. & 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
  • 9
    • 0028241785 scopus 로고
    • Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: Spectroscopic and functional characterization
    • Ferrer, J. C., Turano, P., Banci, L., Bertini, I., Morris, I. K., Smith, K. M., Smith, M. & Mauk, A. G. (1994) Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization, Biochemistry 33, 7819-7829.
    • (1994) Biochemistry , vol.33 , pp. 7819-7829
    • Ferrer, J.C.1    Turano, P.2    Banci, L.3    Bertini, I.4    Morris, I.K.5    Smith, K.M.6    Smith, M.7    Mauk, A.G.8
  • 11
    • 0028810144 scopus 로고
    • pH, electrolyte, and substrate-linked variation in active site structure of the Trp51Ala variant of cytochrome c peroxidase
    • Turano, P., Ferrer, J. C., Cheesman, M. R., Thompson, A. J., Banci, L., Bertini, I. & Mauk, A. G. (1995) pH, electrolyte, and substrate-linked variation in active site structure of the Trp51Ala variant of cytochrome c peroxidase, Biochemistry 34, 13895-13905.
    • (1995) Biochemistry , vol.34 , pp. 13895-13905
    • Turano, P.1    Ferrer, J.C.2    Cheesman, M.R.3    Thompson, A.J.4    Banci, L.5    Bertini, I.6    Mauk, A.G.7
  • 12
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution
    • Finzel, B. C., Poulos, T. L. & 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
  • 13
    • 0026454818 scopus 로고
    • Effect of Asp235→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. & Kraut, J. (1992) Effect of Asp235→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
  • 14
    • 0023692657 scopus 로고
    • Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroseopy
    • Smulevich, G., Mauro, J. M., Fishel, L. A., English, A. M., Kraut, J. & Spiro, T. G. (1988) Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroseopy, Biochemistry 27, 5477-5485.
    • (1988) Biochemistry , vol.27 , pp. 5477-5485
    • Smulevich, G.1    Mauro, J.M.2    Fishel, L.A.3    English, A.M.4    Kraut, J.5    Spiro, T.G.6
  • 15
    • 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. & 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
  • 16
    • 0028076456 scopus 로고
    • A structure of oxyperoxidase as a model for the transient enzyme:peroxide complex
    • Miller, M. A., Shaw, A. & Kraut, J. (1994) A structure of oxyperoxidase as a model for the transient enzyme:peroxide complex, Nat. Struct. Biol. 1, 524-531.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 524-531
    • Miller, M.A.1    Shaw, A.2    Kraut, J.3
  • 18
    • 0023663345 scopus 로고
    • Crystal structure of cytochrome c peroxidase compound I
    • Edwards, S. L., Xuong, N. H., Hamlin, R. C. & Kraut, J. (1987) Crystal structure of cytochrome c peroxidase compound I, Biochemistry 26, 1503-1511.
    • (1987) Biochemistry , vol.26 , pp. 1503-1511
    • Edwards, S.L.1    Xuong, N.H.2    Hamlin, R.C.3    Kraut, J.4
  • 19
    • 0006739227 scopus 로고
    • A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle
    • de Duve, C. (1948) A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle, Acta Chem. Scand. 2, 264-289.
    • (1948) Acta Chem. Scand. , vol.2 , pp. 264-289
    • De Duve, C.1
  • 21
    • 49049126489 scopus 로고
    • Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence
    • Inubushi, T. & Becker, E. D. (1983) Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence, J. Magn. Reson. 51, 128-133.
    • (1983) J. Magn. Reson. , vol.51 , pp. 128-133
    • Inubushi, T.1    Becker, E.D.2
  • 22
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional N.M.R. spectroseopy
    • Macura, S. & Ernst, R. R. (1980) Elucidation of cross relaxation in liquids by two-dimensional N.M.R. spectroseopy, Mol. Phys. 41, 95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 25
    • 0000806424 scopus 로고
    • 'Blue' copper containing oxidases
    • Spiro, T. G., ed. J. Wiley & Sons, New York
    • Reinhammar, B. & Malmström, B. G. (1981) 'Blue' copper containing oxidases, in Copper proteins (Spiro, T. G., ed.) pp. 109-149, J. Wiley & Sons, New York.
    • (1981) Copper Proteins , pp. 109-149
    • Reinhammar, B.1    Malmström, B.G.2
  • 26
    • 0025093186 scopus 로고
    • Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome c
    • Rafferty, S. P., Pearce, L. L., Barker, P. D., Guillemette, J. G., Kay, C. M., Smith, M. & Mauk, A. G. (1990) Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome c, Biochemistry 29, 9365-9369.
    • (1990) Biochemistry , vol.29 , pp. 9365-9369
    • Rafferty, S.P.1    Pearce, L.L.2    Barker, P.D.3    Guillemette, J.G.4    Kay, C.M.5    Smith, M.6    Mauk, A.G.7
  • 27
    • 0020479811 scopus 로고
    • The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism
    • Kang, D. S. & 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
  • 28
    • 0013816680 scopus 로고
    • Studies on cytochrome c peroxidase. I. Purification and some properties
    • Yonetani, T. & Ray, G. S. (1965) Studies on cytochrome c peroxidase. I. Purification and some properties, J. Biol. Chem. 240, 4503-4508.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4503-4508
    • Yonetani, T.1    Ray, G.S.2
  • 29
    • 2142673905 scopus 로고
    • Titration methods: Oxidation-reduction reactions
    • Interscience, New York
    • Kolthoff, I. M. & Belcher, R. (1957) Titration methods: Oxidation-reduction reactions, 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
  • 30
    • 0029126465 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. & 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, 9985-9990.
    • (1995) Biochemistry , vol.34 , pp. 9985-9990
    • Matthis, A.L.1    Erman, J.E.2
  • 31
    • 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. & 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
  • 32
    • 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. & 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
  • 33
    • 0026094705 scopus 로고
    • Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: Resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase
    • Smulevich, G., Miller, M. A., Kraut, J. & Spiro, T. G. (1991) Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase, Biochemistry 30, 9546-9558.
    • (1991) Biochemistry , vol.30 , pp. 9546-9558
    • Smulevich, G.1    Miller, M.A.2    Kraut, J.3    Spiro, T.G.4
  • 34
    • 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. & 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
  • 35
    • 0001215890 scopus 로고
    • Nuclear magnetic resonance of paramagnetic metalloproteins
    • Bertini, I., Turano, P. & Vila, A. J. (1993) Nuclear magnetic resonance of paramagnetic metalloproteins, Chem. Rev. 93, 2833-2932.
    • (1993) Chem. Rev. , vol.93 , pp. 2833-2932
    • Bertini, I.1    Turano, P.2    Vila, A.J.3
  • 36
    • 0019044035 scopus 로고
    • Proton magnetic resonance studies of cytochrome c peroxidase: PD dependence of the isotropically shifted resonances
    • Satterlee, J. D. & Erman, J. E. (1980) Proton magnetic resonance studies of cytochrome c peroxidase: pD dependence of the isotropically shifted resonances, Arch. Biochem. Biophys. 202, 608-616.
    • (1980) Arch. Biochem. Biophys. , vol.202 , pp. 608-616
    • Satterlee, J.D.1    Erman, J.E.2
  • 37
    • 0027339793 scopus 로고
    • 1H fermi contant shifts in horse cytochrome c. The origin of anti-Curie effect
    • 1H fermi contant shifts in horse cytochrome c. The origin of anti-Curie effect, Eur. J. Biochem. 211, 563-568.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 563-568
    • Turner, D.L.1
  • 38
    • 33751154489 scopus 로고
    • 1H contact shifts in low-spin Fe(III) model hemes and heme proteins: Explanations of 'Curie' and 'Anti-Curie' behaviour within the same molecule
    • 1H contact shifts in low-spin Fe(III) model hemes and heme proteins: explanations of 'Curie' and 'Anti-Curie' behaviour within the same molecule, J. Phys. Chem. 99, 17795-17804.
    • (1995) J. Phys. Chem. , vol.99 , pp. 17795-17804
    • Shokhirev, N.V.1    Walker, F.A.2
  • 40
    • 0026611621 scopus 로고
    • 1H NMR investigation of manganese peroxidase from Phanerochaete chrysosporium. A comparison with other peroxidases
    • 1H NMR investigation of manganese peroxidase from Phanerochaete chrysosporium. A comparison with other peroxidases, Biochemistry 31, 10009-10017.
    • (1992) Biochemistry , vol.31 , pp. 10009-10017
    • Banci, L.1    Bertini, I.2    Pease, E.A.3    Tien, M.4    Turano, P.5
  • 41
    • 0027724416 scopus 로고
    • NMR investigation of isotopically labeled cyanide derivatives of lignin peroxidase and manganese peroxidase
    • Banci, L., Bertini, I., Kuan, I.-C., Tien, M., Turano, P. & Vila, A. J. (1993) NMR investigation of isotopically labeled cyanide derivatives of lignin peroxidase and manganese peroxidase, Biochemistry 32, 13483-13489.
    • (1993) Biochemistry , vol.32 , pp. 13483-13489
    • Banci, L.1    Bertini, I.2    Kuan, I.-C.3    Tien, M.4    Turano, P.5    Vila, A.J.6
  • 42
    • 0025873366 scopus 로고
    • Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects
    • Satterlee, J. D. & Erman, J. E. (1991) Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects, Biochemistry 30, 4398-4405.
    • (1991) Biochemistry , vol.30 , pp. 4398-4405
    • Satterlee, J.D.1    Erman, J.E.2
  • 43
    • 0001290915 scopus 로고
    • Proton NMR characterization of the catalytically relevant proximal and distal hydrogen-bonding networks in ligated resting state horseradish peroxidase
    • Thanabal, V., de Ropp, J. S. & La Mar, G. N. (1988) Proton NMR characterization of the catalytically relevant proximal and distal hydrogen-bonding networks in ligated resting state horseradish peroxidase, J. Am. Chem. Soc. 110, 3027-3035.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3027-3035
    • Thanabal, V.1    De Ropp, J.S.2    La Mar, G.N.3
  • 44
    • 0025766930 scopus 로고
    • Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase
    • Banci, L., Bertini, I., Turano, P., Tien, M. & Kirk, T. K. (1991) Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase, Proc. Natl Acad. Sci. USA 88, 6956-6960.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6956-6960
    • Banci, L.1    Bertini, I.2    Turano, P.3    Tien, M.4    Kirk, T.K.5
  • 45
    • 0021933539 scopus 로고
    • Thermal denaturation of cytochrome c peroxidase: PH dependence
    • Gross, M. T. & Erman, J. E. (1985) Thermal denaturation of cytochrome c peroxidase: pH dependence, Biochim. Biophys. Acta 830, 140-146.
    • (1985) Biochim. Biophys. Acta , vol.830 , pp. 140-146
    • Gross, M.T.1    Erman, J.E.2
  • 46
    • 0024278461 scopus 로고
    • Calorimetric studies of the thermal denaturation of cytochrome c peroxidase
    • Kresheck, G. C. & Erman, J. E. (1988) Calorimetric studies of the thermal denaturation of cytochrome c peroxidase, Biochemistry 27, 2490-2496.
    • (1988) Biochemistry , vol.27 , pp. 2490-2496
    • Kresheck, G.C.1    Erman, J.E.2
  • 47
    • 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. & 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
  • 48
    • 0016690880 scopus 로고
    • The oxidation of cytochrome c peroxidase by hydrogen peroxide. Characterization of products
    • Erman, J. E. & Yonetani, T. (1975) 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
  • 49
    • 0016833424 scopus 로고
    • A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound
    • Erman, J. E. & Yonetani, T. (1975) A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound, Biochim. Biophys. Acta 393, 350-357.
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 350-357
    • Erman, J.E.1    Yonetani, T.2
  • 51
    • 0028913020 scopus 로고
    • Identification of a porphyrin π-cation radical in ascorbate peroxidase compound I
    • Patterson, W. R., Poulos, T. L. & Goodin, D. B. (1995) Identification of a porphyrin π-cation radical in ascorbate peroxidase compound I, Biochemistry 34, 4342-4345.
    • (1995) Biochemistry , vol.34 , pp. 4342-4345
    • Patterson, W.R.1    Poulos, T.L.2    Goodin, D.B.3
  • 52
    • 0027316225 scopus 로고
    • Comprehensive explanation of the anomalous EPR spectra of wild-type and mutant cytochrome c peroxidase compound ES
    • Houseman, A. L. P., Doan, P. E., Goodin, D. B. & Hoffman, B. M. (1993) Comprehensive explanation of the anomalous EPR spectra of wild-type and mutant cytochrome c peroxidase compound ES, Biochemistry 32, 4430-4443.
    • (1993) Biochemistry , vol.32 , pp. 4430-4443
    • Houseman, A.L.P.1    Doan, P.E.2    Goodin, D.B.3    Hoffman, B.M.4
  • 53
    • 0023653379 scopus 로고
    • A stopped-flow study of the reaction of cytochrome c peroxidase with hydroperoxides
    • Balny, C., Anni, H. & Yonetani, T. (1987) A stopped-flow study of the reaction of cytochrome c peroxidase with hydroperoxides, FEBS Lett. 221, 349-354.
    • (1987) FEBS Lett. , vol.221 , pp. 349-354
    • Balny, C.1    Anni, H.2    Yonetani, T.3
  • 54
    • 0016693267 scopus 로고
    • A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength
    • Loo, S. & Erman, J. E. (1475) A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength, Biochemistry 14, 3467-3470.
    • (1475) Biochemistry , vol.14 , pp. 3467-3470
    • Loo, S.1    Erman, J.E.2
  • 55
    • 0025270731 scopus 로고
    • Ligand binding and structural perturbations in cytochrome c peroxidase. A crystallographic study
    • Edwards, S. L. & Poulos, T. L. (1990) Ligand binding and structural perturbations in cytochrome c peroxidase. A crystallographic study, J. Biol. Chem. 265, 2588-2595.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2588-2595
    • Edwards, S.L.1    Poulos, T.L.2
  • 56
    • 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. & 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
  • 57
    • 0024373526 scopus 로고
    • Effects of temperature and glycerol on the resonance Raman spectra of cytochrome c peroxidase and selected mutants
    • Smulevich, G., Mantini, A. R., English, A. M. & Mauro, J. M. (1989) Effects of temperature and glycerol on the resonance Raman spectra of cytochrome c peroxidase and selected mutants, Biochemistry 28, 5058-5064.
    • (1989) Biochemistry , vol.28 , pp. 5058-5064
    • Smulevich, G.1    Mantini, A.R.2    English, A.M.3    Mauro, J.M.4
  • 58
    • 0024495355 scopus 로고
    • Effects of buried ionizable aminoacids on the reduction potential of recombinant myoglobin
    • Varadarajan, R., Zewert, T. E., Gray, H. B & Boxer, S. G. (1989) Effects of buried ionizable aminoacids on the reduction potential of recombinant myoglobin, Science 243, 69-72.
    • (1989) Science , vol.243 , pp. 69-72
    • Varadarajan, R.1    Zewert, T.E.2    Gray, H.B.3    Boxer, S.G.4
  • 59
    • 0024594073 scopus 로고
    • Electrostatic interactions in wild-type and mutant recombinant human myoglobins
    • Varadarajan, R., Lambright, D. G. & Boxer, S. G. (1989) Electrostatic interactions in wild-type and mutant recombinant human myoglobins, Biochemistry 28, 3771-3781.
    • (1989) Biochemistry , vol.28 , pp. 3771-3781
    • Varadarajan, R.1    Lambright, D.G.2    Boxer, S.G.3
  • 60
    • 0029637916 scopus 로고
    • Compund ES of cytochrome c peroxidase contains a Trp π-cation radical: Characterization by CW and pulsed Q-band ENDOR spectroscopy
    • Huyett, J. E., Doan, P. E., Gurbiel, R., Houseman, A. L. P., Sivaraja, M., Goodin, D. B. & Hoffman, B. M. (1995) Compund ES of cytochrome c peroxidase contains a Trp π-cation radical: characterization by CW and pulsed Q-band ENDOR spectroscopy, J. Am. Chem. Soc. 117, 9033-9041.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9033-9041
    • Huyett, J.E.1    Doan, P.E.2    Gurbiel, R.3    Houseman, A.L.P.4    Sivaraja, M.5    Goodin, D.B.6    Hoffman, B.M.7
  • 61
    • 0028209418 scopus 로고
    • Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase
    • Fitzgerald, M. M., Churchill, M. J., McRee, D. E. & Goodin, D. B. (1994) Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase, Biochemistry 33, 3807-3818.
    • (1994) Biochemistry , vol.33 , pp. 3807-3818
    • Fitzgerald, M.M.1    Churchill, M.J.2    McRee, D.E.3    Goodin, D.B.4
  • 62
    • 0024430072 scopus 로고
    • Detection of an oxyferryl 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. & Kraut, J. (1989) Detection of an oxyferryl 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
  • 63
    • 0029114694 scopus 로고
    • The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase
    • Fitzgerald, M. M., Trester, M. L., Jensen, G. M., McRee, D. E. & Goodin, D. B. (1995) The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase, Protein Sci. 4, 1844-1850.
    • (1995) Protein Sci. , vol.4 , pp. 1844-1850
    • Fitzgerald, M.M.1    Trester, M.L.2    Jensen, G.M.3    McRee, D.E.4    Goodin, D.B.5
  • 64
    • 0028046894 scopus 로고
    • A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase
    • Miller, M. A., Han, G. W. & Kraut, J. (1994) A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase, Proc. Natl Acad. Sci. USA 91, 11 118-11 122.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11118-11122
    • Miller, M.A.1    Han, G.W.2    Kraut, J.3
  • 65
    • 0026193133 scopus 로고
    • 2D NMR of paramagnetic metalloenzymes: Cyanide-inhibited horseradish peroxidase
    • de Ropp, J. S., Yu, L. P. & La Mar, G. N. (1991) 2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase, J. Biomol. NMR 1, 175-190.
    • (1991) J. Biomol. NMR , vol.1 , pp. 175-190
    • De Ropp, J.S.1    Yu, L.P.2    La Mar, G.N.3
  • 66
    • 0027962802 scopus 로고
    • 2D NMR approaches to characterizing the molecular structure and dynamic stability of the active site for cyanide-inhibited horseradish peroxidase
    • Chen, Z., de Ropp, J. S., Hernández, G. & La Mar, G. N. (1994) 2D NMR approaches to characterizing the molecular structure and dynamic stability of the active site for cyanide-inhibited horseradish peroxidase, J. Am. Chem. Soc. 116, 8772-8783.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8772-8783
    • Chen, Z.1    De Ropp, J.S.2    Hernández, G.3    La Mar, G.N.4
  • 67
    • 0029347077 scopus 로고
    • Factoring of the hyperfine shifts in the cyanide adduct of lignin peroxidase from P. chrysosporium
    • Banci, L., Bertini, I., Pierattelli, R., Tien, M. & Vila, A. J. (1995) Factoring of the hyperfine shifts in the cyanide adduct of lignin peroxidase from P. chrysosporium, J. Am. Chem. Soc. 117, 8659-8667.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8659-8667
    • Banci, L.1    Bertini, I.2    Pierattelli, R.3    Tien, M.4    Vila, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.