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Volumn 1655, Issue 1-3, 2004, Pages 116-122

The function and characteristics of tyrosyl radical cofactors

Author keywords

Amino acid radical; De novo protein; Oxygen evolution; Protein design; Tyrosyl radical; Water oxidation

Indexed keywords

AMINO ACID; CYTOCHROME C OXIDASE; PROTON; RADICAL; TRYPTOPHAN; TYROSINE; WATER;

EID: 1942504811     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.10.017     Document Type: Review
Times cited : (54)

References (57)
  • 1
    • 0002891361 scopus 로고    scopus 로고
    • Oxygen production in nature: A light-driven metalloradical enzyme process
    • Tommos C., Babcock G.T. Oxygen production in nature: a light-driven metalloradical enzyme process. Acc. Chem. Res. 31:1998;18-25.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 18-25
    • Tommos, C.1    Babcock, G.T.2
  • 3
    • 0015760626 scopus 로고
    • Electron paramagnetic resonance signal II in spinach chloroplasts: I. Kinetic analysis for untreated chloroplasts
    • Babcock G.T., Sauer K. Electron paramagnetic resonance signal II in spinach chloroplasts: I. Kinetic analysis for untreated chloroplasts. Biochim. Biophys. Acta. 325:1973;483-503.
    • (1973) Biochim. Biophys. Acta , vol.325 , pp. 483-503
    • Babcock, G.T.1    Sauer, K.2
  • 4
    • 0016429902 scopus 로고
    • A rapid light-induced transient in electron paramagnetic resonance signal II activated upon inhibition of photosynthetic oxygen evolution
    • Babcock G.T., Sauer K. A rapid light-induced transient in electron paramagnetic resonance signal II activated upon inhibition of photosynthetic oxygen evolution. Biochim. Biophys. Acta. 376:1975;315-328.
    • (1975) Biochim. Biophys. Acta , vol.376 , pp. 315-328
    • Babcock, G.T.1    Sauer, K.2
  • 5
    • 0016433801 scopus 로고
    • The rapid component of electron paramagnetic resonance signal II: A candidate for the physiological donor to photosystem II in spinach chloroplasts
    • Babcock G.T., Sauer K. The rapid component of electron paramagnetic resonance signal II: a candidate for the physiological donor to photosystem II in spinach chloroplasts. Biochim. Biophys. Acta. 376:1975;329-344.
    • (1975) Biochim. Biophys. Acta , vol.376 , pp. 329-344
    • Babcock, G.T.1    Sauer, K.2
  • 6
    • 0016612390 scopus 로고
    • Observation of a new EPR transient in chloroplasts that may reflect the electron donor to photosystem II at room temperature
    • Blankenship R.E., Babcock G.T., Warden J.T., Sauer K. Observation of a new EPR transient in chloroplasts that may reflect the electron donor to photosystem II at room temperature. FEBS Lett. 51:1975;287-293.
    • (1975) FEBS Lett. , vol.51 , pp. 287-293
    • Blankenship, R.E.1    Babcock, G.T.2    Warden, J.T.3    Sauer, K.4
  • 8
    • 0017277681 scopus 로고
    • Reaction kinetics for positive charge accumulation on the water side of chloroplast photosystem II
    • Babcock G.T., Blankenship R.E., Sauer K. Reaction kinetics for positive charge accumulation on the water side of chloroplast photosystem II. FEBS Lett. 61:1976;286-289.
    • (1976) FEBS Lett. , vol.61 , pp. 286-289
    • Babcock, G.T.1    Blankenship, R.E.2    Sauer, K.3
  • 9
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes. EPR and electron-transport properties
    • Berthold D.A., Babcock G.T., Yocum C.F. A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes. EPR and electron-transport properties. FEBS Lett. 134:1981;231-234.
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 10
    • 0001473212 scopus 로고
    • + decay kinetics in tris-washed chloroplast photosystem II preparations as a function of pH
    • + decay kinetics in tris-washed chloroplast photosystem II preparations as a function of pH. Biochim. Biophys. Acta. 772:1983;327-330.
    • (1983) Biochim. Biophys. Acta , vol.772 , pp. 327-330
    • Boska, M.1    Sauer, K.2    Buttner, W.3    Babcock, G.T.4
  • 12
    • 18644372534 scopus 로고    scopus 로고
    • Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II
    • Fromme P., Kern J., Loll B., Biesiadka J., Saenger W., Witt H.T., Krauß N., Zouni A. Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II. Philos. Trans. R. Soc. Lond., B. 357:2002;1337-1345.
    • (2002) Philos. Trans. R. Soc. Lond., B , vol.357 , pp. 1337-1345
    • Fromme, P.1    Kern, J.2    Loll, B.3    Biesiadka, J.4    Saenger, W.5    Witt, H.T.6    Krauß, N.7    Zouni, A.8
  • 13
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution
    • Kamiya N., Shen J.-R. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution. Proc. Natl. Acad. Sci. U. S. A. 100:2003;98-103.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 16
    • 0033539481 scopus 로고    scopus 로고
    • How oxygen is activated and reduced in respiration
    • Babcock G.T. How oxygen is activated and reduced in respiration. Proc. Natl. Acad. Sci. U. S. A. 96:1999;12971-12973.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12971-12973
    • Babcock, G.T.1
  • 18
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
    • Proshlyakov D.A., Pressler M.A., DeMaso C., Leykam J.F., DeWitt D.L., Babcock G.T. Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244. Science. 290:2000;1588-1591.
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2    Demaso, C.3    Leykam, J.F.4    Dewitt, D.L.5    Babcock, G.T.6
  • 19
    • 0032318376 scopus 로고    scopus 로고
    • Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine
    • Gennis R.B. Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine. Biochim. Biophys. Acta. 1365:1998;241-248.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 241-248
    • Gennis, R.B.1
  • 20
    • 0032558999 scopus 로고    scopus 로고
    • Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen
    • Sucheta A., Szundi I., Einarsdóttir Ó. Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen. Biochemistry. 37:1998;17905-17914.
    • (1998) Biochemistry , vol.37 , pp. 17905-17914
    • Sucheta, A.1    Szundi, I.2    Einarsdóttir, Ó.3
  • 21
    • 0033587483 scopus 로고    scopus 로고
    • Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide
    • MacMillan F., Kannt A., Behr J., Prisner T., Michel H. Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide. Biochemistry. 38:1999;9179-9184.
    • (1999) Biochemistry , vol.38 , pp. 9179-9184
    • MacMillan, F.1    Kannt, A.2    Behr, J.3    Prisner, T.4    Michel, H.5
  • 23
    • 0038604805 scopus 로고    scopus 로고
    • Free radical catalysis by galactose oxidase
    • Whittaker J.W. Free radical catalysis by galactose oxidase. Chem. Rev. 103:2003;2347-2363.
    • (2003) Chem. Rev. , vol.103 , pp. 2347-2363
    • Whittaker, J.W.1
  • 24
    • 0000787972 scopus 로고
    • 2H electron spin echo envelope modulation (ESEEM) spectroscopic analysis of hydrogen hyperfine interactions
    • 2H electron spin echo envelope modulation (ESEEM) spectroscopic analysis of hydrogen hyperfine interactions. J. Am. Chem. Soc. 116:1994;7332-7340.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7332-7340
    • Warncke, K.1    Babcock, G.T.2    McCracken, J.3
  • 25
    • 0031587471 scopus 로고    scopus 로고
    • Determination of the electron spin density on the phenolic oxygen of the tyrosyl radical of photosystem II
    • Dole F., Diner B.A., Hoganson C.W., Babcock G.T., Britt R.D. Determination of the electron spin density on the phenolic oxygen of the tyrosyl radical of photosystem II. J. Am. Chem. Soc. 119:1997;11540-11541.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11540-11541
    • Dole, F.1    Diner, B.A.2    Hoganson, C.W.3    Babcock, G.T.4    Britt, R.D.5
  • 27
    • 0029904196 scopus 로고    scopus 로고
    • Electron magnetic resonance of the tyrosyl radical in ribonucleotide reductase from Escherichia Coli
    • Hoganson C.W., Sahlin M., Sjöberg B.-M., Babcock G.T. Electron magnetic resonance of the tyrosyl radical in ribonucleotide reductase from Escherichia Coli. J. Am. Chem. Soc. 118:1996;4672-4679.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 4672-4679
    • Hoganson, C.W.1    Sahlin, M.2    Sjöberg, B.-M.3    Babcock, G.T.4
  • 30
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • Tommos C., Babcock G.T. Proton and hydrogen currents in photosynthetic water oxidation. Biochim. Biophys. Acta. 1458:2000;199-219.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 199-219
    • Tommos, C.1    Babcock, G.T.2
  • 32
    • 0037192147 scopus 로고    scopus 로고
    • Crystal structure of the di-iron/radical protein of ribonucleotide reductase from corynebacterium ammoniagenes
    • Högbom M., Huque Y., Sjöberg B.-M., Nordlund P. Crystal structure of the di-iron/radical protein of ribonucleotide reductase from corynebacterium ammoniagenes. Biochemistry. 41:2002;1381-1389.
    • (2002) Biochemistry , vol.41 , pp. 1381-1389
    • Högbom, M.1    Huque, Y.2    Sjöberg, B.-M.3    Nordlund, P.4
  • 34
    • 0027762443 scopus 로고
    • Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center
    • Tang X.-S., Chisholm D.A., Dismukes G.C., Brudvig G.W., Diner B.A. Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center. Biochemistry. 32:1993;13742-13748.
    • (1993) Biochemistry , vol.32 , pp. 13742-13748
    • Tang, X.-S.1    Chisholm, D.A.2    Dismukes, G.C.3    Brudvig, G.W.4    Diner, B.A.5
  • 36
    • 0030734034 scopus 로고    scopus 로고
    • Fourier transform infrared difference spectroscopy of photosystem II tyrosine D using site-directed mutagenesis and specific isotope labeling
    • Hienerwadel R., Boussac A., Breton J., Diner B.A., Berthomieu C. Fourier transform infrared difference spectroscopy of photosystem II tyrosine D using site-directed mutagenesis and specific isotope labeling. Biochemistry. 36:1997;14712-14723.
    • (1997) Biochemistry , vol.36 , pp. 14712-14723
    • Hienerwadel, R.1    Boussac, A.2    Breton, J.3    Diner, B.A.4    Berthomieu, C.5
  • 37
    • 0032517368 scopus 로고    scopus 로고
    • Stepwise disintegration of the photosynthetic oxygen-evolving complex
    • Tommos C., McCracken J., Styring S., Babcock G.T. Stepwise disintegration of the photosynthetic oxygen-evolving complex. J. Am. Chem. Soc. 120:1998;10441-10452.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10441-10452
    • Tommos, C.1    McCracken, J.2    Styring, S.3    Babcock, G.T.4
  • 38
    • 0037195341 scopus 로고    scopus 로고
    • Electron, proton and hydrogen-atom transfers in photosynthetic water oxidation
    • Tommos C. Electron, proton and hydrogen-atom transfers in photosynthetic water oxidation. Philos. Trans. R. Soc. Lond., B. 357:2002;1383-1394.
    • (2002) Philos. Trans. R. Soc. Lond., B , vol.357 , pp. 1383-1394
    • Tommos, C.1
  • 39
    • 0035808702 scopus 로고    scopus 로고
    • Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation
    • Diner B.A. Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation. Biochim. Biophys. Acta. 1503:2001;147-163.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 147-163
    • Diner, B.A.1
  • 40
    • 0035808665 scopus 로고    scopus 로고
    • Z and the manganese cluster in the water oxidizing complex of photosystem II
    • Z and the manganese cluster in the water oxidizing complex of photosystem II. Biochim. Biophys. Acta. 1503:2001;164-186.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 164-186
    • Debus, R.J.1
  • 43
    • 0035808688 scopus 로고    scopus 로고
    • Coupling of electron and proton transfer in the photosynthetic water oxidase
    • Rappaport F., Lavergne J. Coupling of electron and proton transfer in the photosynthetic water oxidase. Biochim. Biophys. Acta. 1503:2001;246-259.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 246-259
    • Rappaport, F.1    Lavergne, J.2
  • 46
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • Hoganson C.W., Babcock G.T. A metalloradical mechanism for the generation of oxygen from water in photosynthesis. Science. 277:1997;1953-1956.
    • (1997) Science , vol.277 , pp. 1953-1956
    • Hoganson, C.W.1    Babcock, G.T.2
  • 49
    • 0032575296 scopus 로고    scopus 로고
    • Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: Structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins
    • Logan D.T., deMaré F., Persson B.O., Slaby A., Sjöberg B.-M., Nordlund P. Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins. Biochemistry. 37:1998;10798-10807.
    • (1998) Biochemistry , vol.37 , pp. 10798-10807
    • Logan, D.T.1    Demaré, F.2    Persson, B.O.3    Slaby, A.4    Sjöberg, B.-M.5    Nordlund, P.6
  • 51
    • 0030608718 scopus 로고    scopus 로고
    • · reduction kinetics in the absence of the manganese-stabilizing protein of photosystem II
    • · reduction kinetics in the absence of the manganese-stabilizing protein of photosystem II. Biochemistry. 36:1997;14474-14478.
    • (1997) Biochemistry , vol.36 , pp. 14474-14478
    • Razeghifard, M.R.1    Wydrzynski, T.2    Pace, R.J.3    Burnap, R.L.4
  • 57
    • 0033544354 scopus 로고    scopus 로고
    • Cation-π interactions in proteins: Can simple models provide an accurate description?
    • Minoux H., Chipot C. Cation-π interactions in proteins: can simple models provide an accurate description? J. Am. Chem. Soc. 121:1999;10366-10372.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10366-10372
    • Minoux, H.1    Chipot, C.2


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