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Volumn 1834, Issue 1, 2013, Pages 137-148

Apolar distal pocket mutants of yeast cytochrome c peroxidase: Hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants

Author keywords

Cyanide binding; Cytochrome c peroxidase; Distal pocket mutant; Hydrogen peroxide reaction; Spectroscopic property

Indexed keywords

ALANINE; CYANIDE; CYTOCHROME C PEROXIDASE; HEME; HISTIDINE; HYDROGEN PEROXIDE; LEUCINE; TRYPTOPHAN; VALINE;

EID: 84869861609     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.09.005     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0014010710 scopus 로고
    • Studies on cytochrome c peroxidase IV. A comparison of peroxide-induced complexes of horseradish and cytochrome c peroxidases
    • T. Yonetani Studies on cytochrome c peroxidase IV. A comparison of peroxide-induced complexes of horseradish and cytochrome c peroxidases J. Biol. Chem. 241 1966 2562 2571
    • (1966) J. Biol. Chem. , vol.241 , pp. 2562-2571
    • Yonetani, T.1
  • 3
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution
    • B.C. Finzel, T.L. Poulos, and J. Kraut Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution J. Biol. Chem. 259 1984 13027 13036
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 4
    • 0028587337 scopus 로고
    • The crystal structure of manganese peroxidase from Phanerochaete chrysoporium at 2.06-Å resolution
    • M. Sundaramoorthy, K. Kishi, M.H. Gold, and T.L. Poulos The crystal structure of manganese peroxidase from Phanerochaete chrysoporium at 2.06-Å resolution J. Biol. Chem. 269 1994 32759 32767
    • (1994) J. Biol. Chem. , vol.269 , pp. 32759-32767
    • Sundaramoorthy, M.1    Kishi, K.2    Gold, M.H.3    Poulos, T.L.4
  • 5
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • W.R. Patterson, and T.L. Poulos Crystal structure of recombinant pea cytosolic ascorbate peroxidase Biochemistry 34 1995 4331 4341
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 7
    • 0000313831 scopus 로고
    • Active-site mutations in cytochrome c peroxidase: A critical role for histidine-52 in the rate of formation of compound i
    • J.E. Erman, L.B. Vitello, M.A. Miller, and J. Kraut 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 1992 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
  • 8
    • 0027421337 scopus 로고
    • Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound i
    • J.E. Erman, L.B. Vitello, M.A. Miller, A. Shaw, K.A. Brown, and J. Kraut Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I Biochemistry 32 1993 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
    • 0022020912 scopus 로고
    • The degradation of cytochrome c by hydrogen peroxide
    • T.M. Florence The degradation of cytochrome c by hydrogen peroxide J. Inorg. Biochem. 23 1985 131 141
    • (1985) J. Inorg. Biochem. , vol.23 , pp. 131-141
    • Florence, T.M.1
  • 10
    • 26644473174 scopus 로고    scopus 로고
    • Reactions of peroxynitrite with globin proteins and their possible physiological role
    • S. Herold, and A. Fago Reactions of peroxynitrite with globin proteins and their possible physiological role Comp. Biochem. Physiol. A Mol. Integr. Physiol. 142A 2005 124 129
    • (2005) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.142 A , pp. 124-129
    • Herold, S.1    Fago, A.2
  • 11
    • 79952697177 scopus 로고    scopus 로고
    • Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: Properties of CcP mutants H52D, H52E, H52N, and H52Q
    • M.C. Foshay, L.B. Vitello, and J.E. Erman Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: Properties of CcP mutants H52D, H52E, H52N, and H52Q Biochim. Biophys. Acta 1814 2011 525 535
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 525-535
    • Foshay, M.C.1    Vitello, L.B.2    Erman, J.E.3
  • 13
    • 0025895757 scopus 로고
    • Reactions and significance of cytochrome P-450 enzymes
    • F.P. Guengerich Reactions and significance of cytochrome P-450 enzymes J. Biol. Chem. 266 1991 10019 10022
    • (1991) J. Biol. Chem. , vol.266 , pp. 10019-10022
    • Guengerich, F.P.1
  • 14
    • 0037174181 scopus 로고    scopus 로고
    • Functional modulation of a peroxygenase cytochrome P450: Novel insight into the mechanisms of peroxygenase and peroxidase enzymes
    • I. Matsunaga, T. Sumimoto, M. Ayata, and H. Ogura Functional modulation of a peroxygenase cytochrome P450: novel insight into the mechanisms of peroxygenase and peroxidase enzymes FEBS Lett. 528 2002 90 94
    • (2002) FEBS Lett. , vol.528 , pp. 90-94
    • Matsunaga, I.1    Sumimoto, T.2    Ayata, M.3    Ogura, H.4
  • 15
    • 0015979118 scopus 로고
    • Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase
    • J.E. Erman Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase Biochemistry 13 1974 39 44
    • (1974) Biochemistry , vol.13 , pp. 39-44
    • Erman, J.E.1
  • 16
    • 0035834055 scopus 로고    scopus 로고
    • Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase
    • M.I. Savenkova, J.D. Satterlee, J.E. Erman, W.F. Siems, and G.L. Helms Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase Biochemistry 40 2001 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
  • 17
    • 0019170291 scopus 로고
    • Primary structure of yeast cytochrome c peroxidase II. The complete amino acid sequence
    • K. Takio, K. Titani, L.H. Ericsson, and T. Yonetani Primary structure of yeast cytochrome c peroxidase II. The complete amino acid sequence Arch. Biochem. Biophys. 203 1980 615 629
    • (1980) Arch. Biochem. Biophys. , vol.203 , pp. 615-629
    • Takio, K.1    Titani, K.2    Ericsson, L.H.3    Yonetani, T.4
  • 18
    • 0034130258 scopus 로고    scopus 로고
    • Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly purified holoenzymes
    • J.G. Teske, M.I. Savenkova, J.M. Mauro, J.E. Erman, and J.D. Satterlee Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly purified holoenzymes Protein Expr. Purif. 19 2000 139 147
    • (2000) Protein Expr. 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
  • 19
    • 0023106193 scopus 로고
    • Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound i
    • L.A. Fishel, J.E. Villafranca, J.M. Mauro, and J. Kraut Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I Biochemistry 26 1987 351 360
    • (1987) Biochemistry , vol.26 , pp. 351-360
    • Fishel, L.A.1    Villafranca, J.E.2    Mauro, J.M.3    Kraut, J.4
  • 21
    • 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
    • W.B.R. Pollock, F.I. Rosell, M.B. Twitchett, M.E. Dumont, and A.G. Mauk Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition Biochemistry 37 1998 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
  • 23
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • E.A. Berry, and B.L. Trumpower Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra Anal. Biochem. 161 1987 1 15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 24
    • 40149111566 scopus 로고    scopus 로고
    • Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: Evidence for a single, catalytically active, cytochrome c binding domain
    • N.M. Pearl, T. Jacobson, C. Meyen, A.G. Clementz, E.Y. Ok, E. Choi, K. Wilson, L.B. Vitello, and J.E. Erman Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: evidence for a single, catalytically active, cytochrome c binding domain Biochemistry 47 2008 2766 2775
    • (2008) Biochemistry , vol.47 , pp. 2766-2775
    • Pearl, N.M.1    Jacobson, T.2    Meyen, C.3    Clementz, A.G.4    Ok, E.Y.5    Choi, E.6    Wilson, K.7    Vitello, L.B.8    Erman, J.E.9
  • 25
    • 33845363586 scopus 로고    scopus 로고
    • Speciation and structure of ferriprotoporphyrin IX in aqueous solution: Spectroscopic and diffusion measurements demonstrate dimerization, but not μ-oxo dimer formation
    • K.A. De Villiers, C.H. Kaschula, T.J. Egan, and H.M. Marques Speciation and structure of ferriprotoporphyrin IX in aqueous solution: spectroscopic and diffusion measurements demonstrate dimerization, but not μ-oxo dimer formation J. Biol. Inorg. Chem. 12 2007 101 117
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 101-117
    • De Villiers, K.A.1    Kaschula, C.H.2    Egan, T.J.3    Marques, H.M.4
  • 26
    • 0016693267 scopus 로고
    • A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength
    • S. Loo, and J.E. Erman A kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength Biochemistry 14 1975 3467 3470
    • (1975) Biochemistry , vol.14 , pp. 3467-3470
    • Loo, S.1    Erman, J.E.2
  • 27
    • 34447547742 scopus 로고    scopus 로고
    • 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
    • N.M. Pearl, T. Jacobson, M. Arisa, L.B. Vitello, and J.E. Erman 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 Biochemistry 46 2007 8263 8272
    • (2007) Biochemistry , vol.46 , pp. 8263-8272
    • Pearl, N.M.1    Jacobson, T.2    Arisa, M.3    Vitello, L.B.4    Erman, J.E.5
  • 28
    • 0014010171 scopus 로고
    • Studies on cytochrome c peroxidase. III. Kinetics of the peroxidatic oxidation of ferrocytochrome c catalyzed by cytochrome c peroxidase
    • T. Yonetani, and G.S. Ray Studies on cytochrome c peroxidase. III. Kinetics of the peroxidatic oxidation of ferrocytochrome c catalyzed by cytochrome c peroxidase J. Biol. Chem. 241 1966 700 706
    • (1966) J. Biol. Chem. , vol.241 , pp. 700-706
    • Yonetani, T.1    Ray, G.S.2
  • 29
    • 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
    • A.L. Matthis, and J.E. Erman Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters Biochemistry 34 1995 9985 9990
    • (1995) Biochemistry , vol.34 , pp. 9985-9990
    • Matthis, A.L.1    Erman, J.E.2
  • 30
    • 0029751080 scopus 로고    scopus 로고
    • A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase
    • M.A. Miller A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase Biochemistry 35 1996 15791 15799
    • (1996) Biochemistry , vol.35 , pp. 15791-15799
    • Miller, M.A.1
  • 31
    • 0014352643 scopus 로고
    • Analysis of the visible spectra of some sperm-whale ferrimyoglobin derivatives
    • D.W. Smith, and R.J.P. Williams Analysis of the visible spectra of some sperm-whale ferrimyoglobin derivatives Biochem. J. 110 1968 297 301
    • (1968) Biochem. J. , vol.110 , pp. 297-301
    • Smith, D.W.1    Williams, R.J.P.2
  • 32
    • 0014895790 scopus 로고
    • Spin changes in hemoproteins
    • T. Iizuka, and T. Yonetani Spin changes in hemoproteins Adv. Biophys. 1 1970 157 182
    • (1970) Adv. Biophys. , vol.1 , pp. 157-182
    • Iizuka, T.1    Yonetani, T.2
  • 33
    • 0025240820 scopus 로고
    • Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants
    • L.B. Vitello, J.E. Erman, J.M. Mauro, and J. Kraut Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants Biochim. Biophys. Acta 1038 1990 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
  • 34
    • 0025359972 scopus 로고
    • PH-dependent spectral and kinetic properties of cytochrome c peroxidase: Comparison of freshly isolated and stored enzyme
    • L.B. Vitello, M. Huang, and J.E. Erman pH-dependent spectral and kinetic properties of cytochrome c peroxidase: comparison of freshly isolated and stored enzyme Biochemistry 29 1990 4283 4288
    • (1990) Biochemistry , vol.29 , pp. 4283-4288
    • Vitello, L.B.1    Huang, M.2    Erman, J.E.3
  • 35
    • 0027424783 scopus 로고
    • Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide
    • L.B. Vitello, J.E. Erman, M.A. Miller, J. Wang, and J. Kraut Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide Biochemistry 32 1993 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
  • 36
    • 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
    • M.F. Zipplies, W.A. Lee, and T.C. Bruice 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 1986 4433 4445
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 4433-4445
    • Zipplies, M.F.1    Lee, W.A.2    Bruice, T.C.3
  • 40
    • 2142814288 scopus 로고    scopus 로고
    • PH dependence of heme iron coordination, hydrogen peroxide reactivity, and cyanide binding in cytochrome c peroxidase (H52K)
    • M.C. Foshay, L.B. Vitello, and J.E. Erman pH dependence of heme iron coordination, hydrogen peroxide reactivity, and cyanide binding in cytochrome c peroxidase (H52K) Biochemistry 43 2004 5065 5072
    • (2004) Biochemistry , vol.43 , pp. 5065-5072
    • Foshay, M.C.1    Vitello, L.B.2    Erman, J.E.3
  • 41
    • 0016833424 scopus 로고
    • A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound
    • J.E. Erman, and T. Yonetani A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound Biochim. Biophys. Acta 393 1975 350 357
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 350-357
    • Erman, J.E.1    Yonetani, T.2
  • 42
    • 0000313831 scopus 로고
    • Active-site mutations in cytochrome c peroxidase: A critical role for histidine-52 in the rate of formation of compound i
    • J.E. Erman, L.B. Vitello, M.A. Miller, and J. Kraut 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 1992 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


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