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Volumn 112, Issue 35, 2015, Pages 10920-10925

Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage

Author keywords

Cytochrome P450; Electron transfer; Iron oxygenases; Reactive oxygen species; Superoxide dismutase

Indexed keywords

AROMATIC AMINO ACID; CHOLESTEROL MONOOXYGENASE (SIDE CHAIN CLEAVING); CYTOCHROME C OXIDASE; GLYCOSIDASE; HYDROLASE; ISOMERASE; LIGASE; LYASE; METHANE MONOOXYGENASE; MITOCHONDRIAL ENZYME; OXIDOREDUCTASE; PROTEIN; STEROID HORMONE; SUPEROXIDE DISMUTASE; TRANSFERASE; TRYPTOPHAN; TYROSINE;

EID: 84940995096     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1512704112     Document Type: Article
Times cited : (199)

References (51)
  • 1
    • 84894261996 scopus 로고    scopus 로고
    • The rise of oxygen in Earth's early ocean and atmosphere
    • Lyons TW, Reinhard CT, Planavsky NJ (2014) The rise of oxygen in Earth's early ocean and atmosphere. Nature 506(7488):307-315.
    • (2014) Nature , vol.506 , Issue.7488 , pp. 307-315
    • Lyons, T.W.1    Reinhard, C.T.2    Planavsky, N.J.3
  • 3
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies MJ (2005) The oxidative environment and protein damage. Biochim Biophys Acta 1703(2):93-109.
    • (2005) Biochim Biophys Acta , vol.1703 , Issue.2 , pp. 93-109
    • Davies, M.J.1
  • 4
    • 84884179284 scopus 로고    scopus 로고
    • The redox proteome
    • Go Y-M, Jones DP (2013) The redox proteome. J Biol Chem 288(37):26512-26520.
    • (2013) J Biol Chem , vol.288 , Issue.37 , pp. 26512-26520
    • Go, Y.-M.1    Jones, D.P.2
  • 5
    • 84896885938 scopus 로고    scopus 로고
    • Long-range electron tunneling
    • Winkler JR, Gray HB (2014) Long-range electron tunneling. J Am Chem Soc 136(8): 2930-2939.
    • (2014) J Am Chem Soc , vol.136 , Issue.8 , pp. 2930-2939
    • Winkler, J.R.1    Gray, H.B.2
  • 6
    • 84922572228 scopus 로고    scopus 로고
    • Could tyrosine and tryptophan serve multiple roles in biological redox processes?
    • Winkler JR, Gray HB (2015) Could tyrosine and tryptophan serve multiple roles in biological redox processes? Philos Trans R Soc A 373(2037):20140178.
    • (2015) Philos Trans R Soc A , vol.373 , Issue.2037
    • Winkler, J.R.1    Gray, H.B.2
  • 7
    • 84893727993 scopus 로고    scopus 로고
    • Electron flow through metalloproteins
    • Winkler JR, Gray HB (2014) Electron flow through metalloproteins. Chem Rev 114(7): 3369-3380.
    • (2014) Chem Rev , vol.114 , Issue.7 , pp. 3369-3380
    • Winkler, J.R.1    Gray, H.B.2
  • 8
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA, Sutin N (1985) Electron transfers in chemistry and biology. Biochim Biophys Acta 811(3):265-322.
    • (1985) Biochim Biophys Acta , vol.811 , Issue.3 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 9
    • 78650581853 scopus 로고    scopus 로고
    • Proton-coupled electron flow in protein redox machines
    • Dempsey JL, Winkler JR, Gray HB (2010) Proton-coupled electron flow in protein redox machines. Chem Rev 110(12):7024-7039.
    • (2010) Chem Rev , vol.110 , Issue.12 , pp. 7024-7039
    • Dempsey, J.L.1    Winkler, J.R.2    Gray, H.B.3
  • 10
    • 84897987543 scopus 로고    scopus 로고
    • Biochemistry and theory of proton-coupled electron transfer
    • Migliore A, Polizzi NF, Therien MJ, Beratan DN (2014) Biochemistry and theory of proton-coupled electron transfer. Chem Rev 114(7):3381-3465.
    • (2014) Chem Rev , vol.114 , Issue.7 , pp. 3381-3465
    • Migliore, A.1    Polizzi, N.F.2    Therien, M.J.3    Beratan, D.N.4
  • 11
    • 78650530548 scopus 로고    scopus 로고
    • Theory of coupled electron and proton transfer reactions
    • Hammes-Schiffer S, Stuchebrukhov AA (2010) Theory of coupled electron and proton transfer reactions. Chem Rev 110(12):6939-6960.
    • (2010) Chem Rev , vol.110 , Issue.12 , pp. 6939-6960
    • Hammes-Schiffer, S.1    Stuchebrukhov, A.A.2
  • 13
    • 46449093308 scopus 로고    scopus 로고
    • Tryptophan-accelerated electron flow through proteins
    • Shih C, et al. (2008) Tryptophan-accelerated electron flow through proteins. Science 320(5884):1760-1762.
    • (2008) Science , vol.320 , Issue.5884 , pp. 1760-1762
    • Shih, C.1
  • 16
    • 76649102458 scopus 로고    scopus 로고
    • Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance
    • Roessler MM, et al. (2010) Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance. Proc Natl Acad Sci USA 107(5):1930-1935.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.5 , pp. 1930-1935
    • Roessler, M.M.1
  • 17
    • 84872332798 scopus 로고    scopus 로고
    • Energy-converting respiratory Complex I: On the way to the molecular mechanism of the proton pump
    • Verkhovskaya M, Bloch DA (2013) Energy-converting respiratory Complex I: On the way to the molecular mechanism of the proton pump. Int J Biochem Cell Biol 45(2): 491-511.
    • (2013) Int J Biochem Cell Biol , vol.45 , Issue.2 , pp. 491-511
    • Verkhovskaya, M.1    Bloch, D.A.2
  • 18
    • 79953276706 scopus 로고    scopus 로고
    • Calculated vertical ionization energies of the common α-amino acids in the gas phase and in solution
    • Close DM (2011) Calculated vertical ionization energies of the common α-amino acids in the gas phase and in solution. J Phys Chem A 115(13):2900-2912.
    • (2011) J Phys Chem A , vol.115 , Issue.13 , pp. 2900-2912
    • Close, D.M.1
  • 19
    • 55249125700 scopus 로고    scopus 로고
    • Redox proteomics: Basic principles and future perspectives for the detection of protein oxidation in plants
    • Rinalducci S, Murgiano L, Zolla L (2008) Redox proteomics: Basic principles and future perspectives for the detection of protein oxidation in plants. J Exp Bot 59(14): 3781-3801.
    • (2008) J Exp Bot , vol.59 , Issue.14 , pp. 3781-3801
    • Rinalducci, S.1    Murgiano, L.2    Zolla, L.3
  • 20
    • 84877877973 scopus 로고    scopus 로고
    • Reversible, long-range radical transfer in E. coli class Ia ribonucleotide reductase
    • Minnihan EC, Nocera DG, Stubbe J (2013) Reversible, long-range radical transfer in E. coli class Ia ribonucleotide reductase. Acc Chem Res 46(11):2524-2535.
    • (2013) Acc Chem Res , vol.46 , Issue.11 , pp. 2524-2535
    • Minnihan, E.C.1    Nocera, D.G.2    Stubbe, J.3
  • 21
    • 78649642414 scopus 로고    scopus 로고
    • Reaction mechanisms of DNA photolyase
    • Brettel K, Byrdin M (2010) Reaction mechanisms of DNA photolyase. Curr Opin Struct Biol 20(6):693-701.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.6 , pp. 693-701
    • Brettel, K.1    Byrdin, M.2
  • 22
    • 84881430037 scopus 로고    scopus 로고
    • Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: Compensating changes in the electronic coupling and reorganization energies
    • Jiang N, et al. (2013) Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: Compensating changes in the electronic coupling and reorganization energies. J Phys Chem B 117(31):9129-9141.
    • (2013) J Phys Chem B , vol.117 , Issue.31 , pp. 9129-9141
    • Jiang, N.1
  • 23
    • 84858208696 scopus 로고    scopus 로고
    • Two tyrosyl radicals stabilize high oxidation states in cytochrome C oxidase for efficient energy conservation and proton translocation
    • Yu MA, et al. (2012) Two tyrosyl radicals stabilize high oxidation states in cytochrome C oxidase for efficient energy conservation and proton translocation. J Am Chem Soc 134(10):4753-4761.
    • (2012) J Am Chem Soc , vol.134 , Issue.10 , pp. 4753-4761
    • Yu, M.A.1
  • 24
    • 0027078560 scopus 로고
    • Correlation analysis of amino acid usage in protein classes
    • Karlin S, Bucher P (1992) Correlation analysis of amino acid usage in protein classes. Proc Natl Acad Sci USA 89(24):12165-12169.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.24 , pp. 12165-12169
    • Karlin, S.1    Bucher, P.2
  • 25
    • 0028247378 scopus 로고
    • Measuring residue associations in protein structures. Possible implications for protein folding
    • Karlin S, Zuker M, Brocchieri L (1994) Measuring residue associations in protein structures. Possible implications for protein folding. J Mol Biol 239(2):227-248.
    • (1994) J Mol Biol , vol.239 , Issue.2 , pp. 227-248
    • Karlin, S.1    Zuker, M.2    Brocchieri, L.3
  • 26
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley SK, Petsko GA (1985) Aromatic-aromatic interaction: A mechanism of protein structure stabilization. Science 229(4708):23-28.
    • (1985) Science , vol.229 , Issue.4708 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 28
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman HM, et al. (2000) The Protein Data Bank. Nucleic Acids Res 28(1):235-242.
    • (2000) Nucleic Acids Res , vol.28 , Issue.1 , pp. 235-242
    • Berman, H.M.1
  • 29
    • 77952619575 scopus 로고    scopus 로고
    • The electrochemical approach to concerted proton-electron transfers in the oxidation of phenols in water
    • Costentin C, Louault C, Robert M, Savéant JM (2009) The electrochemical approach to concerted proton-electron transfers in the oxidation of phenols in water. Proc Natl Acad Sci USA 106(43):18143-18148.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.43 , pp. 18143-18148
    • Costentin, C.1    Louault, C.2    Robert, M.3    Savéant, J.M.4
  • 30
    • 77952331283 scopus 로고    scopus 로고
    • 2 reduction with minimization of reactive oxygens and provide a proton-pumping gate
    • 2 reduction with minimization of reactive oxygens and provide a proton-pumping gate. Proc Natl Acad Sci USA 107(17):7740-7745.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.17 , pp. 7740-7745
    • Muramoto, K.1
  • 31
    • 0037427449 scopus 로고    scopus 로고
    • The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
    • Strange RW, et al. (2003) The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. J Mol Biol 328(4):877-891.
    • (2003) J Mol Biol , vol.328 , Issue.4 , pp. 877-891
    • Strange, R.W.1
  • 32
    • 64049104165 scopus 로고    scopus 로고
    • The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: Insights into heparin and collagen binding
    • Antonyuk SV, Strange RW, Marklund SL, Hasnain SS (2009) The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: Insights into heparin and collagen binding. J Mol Biol 388(2):310-326.
    • (2009) J Mol Biol , vol.388 , Issue.2 , pp. 310-326
    • Antonyuk, S.V.1    Strange, R.W.2    Marklund, S.L.3    Hasnain, S.S.4
  • 33
    • 0026688441 scopus 로고
    • The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
    • Borgstahl GEO, et al. (1992) The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 71(1):107-118.
    • (1992) Cell , vol.71 , Issue.1 , pp. 107-118
    • Borgstahl, G.E.O.1
  • 34
    • 65249133409 scopus 로고    scopus 로고
    • Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis
    • Perry JJP, et al. (2009) Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis. Biochemistry 48(15):3417-3424.
    • (2009) Biochemistry , vol.48 , Issue.15 , pp. 3417-3424
    • Perry, J.J.P.1
  • 35
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP (2009) How mitochondria produce reactive oxygen species. Biochem J 417(1):1-13.
    • (2009) Biochem J , vol.417 , Issue.1 , pp. 1-13
    • Murphy, M.P.1
  • 38
    • 79959950838 scopus 로고    scopus 로고
    • Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system
    • Strushkevich N, et al. (2011) Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proc Natl Acad Sci USA 108(25):10139-10143.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.25 , pp. 10139-10143
    • Strushkevich, N.1
  • 39
    • 79953148368 scopus 로고    scopus 로고
    • Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1
    • Mast N, et al. (2011) Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1. J Biol Chem 286(7):5607-5613.
    • (2011) J Biol Chem , vol.286 , Issue.7 , pp. 5607-5613
    • Mast, N.1
  • 40
    • 84867515001 scopus 로고    scopus 로고
    • Compound I is the reactive intermediate in the first monooxygenation step during conversion of cholesterol to pregnenolone by cytochrome P450scc: EPR/ENDOR/cryoreduction/annealing studies
    • Davydov R, Gilep AA, Strushkevich NV, Usanov SA, Hoffman BM (2012) Compound I is the reactive intermediate in the first monooxygenation step during conversion of cholesterol to pregnenolone by cytochrome P450scc: EPR/ENDOR/cryoreduction/annealing studies. J Am Chem Soc 134(41):17149-17156.
    • (2012) J Am Chem Soc , vol.134 , Issue.41 , pp. 17149-17156
    • Davydov, R.1    Gilep, A.A.2    Strushkevich, N.V.3    Usanov, S.A.4    Hoffman, B.M.5
  • 41
    • 84887768969 scopus 로고    scopus 로고
    • A selective stepwise heme oxygenase model system: An iron(IV)-oxo porphyrin π-cation radical leads to a verdoheme-type compound via an isoporphyrin intermediate
    • Garcia-Bosch I, Sharma SK, Karlin KD (2013) A selective stepwise heme oxygenase model system: An iron(IV)-oxo porphyrin π-cation radical leads to a verdoheme-type compound via an isoporphyrin intermediate. J Am Chem Soc 135(44):16248-16251.
    • (2013) J Am Chem Soc , vol.135 , Issue.44 , pp. 16248-16251
    • Garcia-Bosch, I.1    Sharma, S.K.2    Karlin, K.D.3
  • 42
    • 0027328115 scopus 로고
    • Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system
    • Hanukoglu I, Rapoport R, Weiner L, Sklan D (1993) Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system. Arch Biochem Biophys 305(2):489-498.
    • (1993) Arch Biochem Biophys , vol.305 , Issue.2 , pp. 489-498
    • Hanukoglu, I.1    Rapoport, R.2    Weiner, L.3    Sklan, D.4
  • 43
    • 78149373621 scopus 로고    scopus 로고
    • Cytochrome P450 compound I: Capture, characterization, and C-H bond activation kinetics
    • Rittle J, Green MT (2010) Cytochrome P450 compound I: Capture, characterization, and C-H bond activation kinetics. Science 330(6006):933-937.
    • (2010) Science , vol.330 , Issue.6006 , pp. 933-937
    • Rittle, J.1    Green, M.T.2
  • 44
    • 84887761225 scopus 로고    scopus 로고
    • Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450
    • Yosca TH, et al. (2013) Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450. Science 342(6160):825-829.
    • (2013) Science , vol.342 , Issue.6160 , pp. 825-829
    • Yosca, T.H.1
  • 45
    • 84922022543 scopus 로고    scopus 로고
    • Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates
    • Williams ST, et al. (2014) Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates. Epigenetics 9(12):1596-1603.
    • (2014) Epigenetics , vol.9 , Issue.12 , pp. 1596-1603
    • Williams, S.T.1
  • 46
    • 0030885887 scopus 로고    scopus 로고
    • Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions
    • Rosenzweig AC, et al. (1997) Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions. Proteins 29(2):141-152.
    • (1997) Proteins , vol.29 , Issue.2 , pp. 141-152
    • Rosenzweig, A.C.1
  • 47
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G, Henrissat B (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3(9):853-859.
    • (1995) Structure , vol.3 , Issue.9 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 48
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas NK (1991) Atomic features of protein-carbohydrate interactions. Curr Opin Struct Biol 1(5):732-740.
    • (1991) Curr Opin Struct Biol , vol.1 , Issue.5 , pp. 732-740
    • Vyas, N.K.1
  • 49
    • 81755186906 scopus 로고    scopus 로고
    • Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation
    • Payne CM, et al. (2011) Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation. J Biol Chem 286(47): 41028-41035.
    • (2011) J Biol Chem , vol.286 , Issue.47 , pp. 41028-41035
    • Payne, C.M.1
  • 51
    • 84885472701 scopus 로고    scopus 로고
    • Recent insights into copper-containing lytic polysaccharide mono-oxygenases
    • Hemsworth GR, Davies GJ, Walton PH (2013) Recent insights into copper-containing lytic polysaccharide mono-oxygenases. Curr Opin Struct Biol 23(5):660-668.
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.5 , pp. 660-668
    • Hemsworth, G.R.1    Davies, G.J.2    Walton, P.H.3


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