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Volumn 403, Issue 3, 2007, Pages 391-395

Ferryl haem protonation gates peroxidatic reactivity in globins

Author keywords

Compound II; Ferryl; Globin; Haemoglobin; Myoglobin; Peroxidase

Indexed keywords

BIOCHEMISTRY; CYTOTOXICITY; ENZYME KINETICS; IRON COMPOUNDS; PH EFFECTS; PROTONATION;

EID: 34247853277     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061421     Document Type: Article
Times cited : (82)

References (48)
  • 1
    • 33645875048 scopus 로고    scopus 로고
    • High-valent iron in chemical and biological oxidations
    • Groves, J. T. (2006) High-valent iron in chemical and biological oxidations. J. Inorg. Biochem. 100, 434-447
    • (2006) J. Inorg. Biochem , vol.100 , pp. 434-447
    • Groves, J.T.1
  • 2
    • 3042710029 scopus 로고    scopus 로고
    • The nature of the high-valent complexes in the catalytic cycles of hemoproteins
    • Silaghi-Dumitrescu, R. (2004) The nature of the high-valent complexes in the catalytic cycles of hemoproteins. J. Biol. Inorg. Chem. 9, 471-476
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 471-476
    • Silaghi-Dumitrescu, R.1
  • 4
    • 0003514551 scopus 로고    scopus 로고
    • John Wiley, New York and Chichester
    • Dunford, H. B. (1999) Heme peroxidases, John Wiley, New York and Chichester
    • (1999) Heme peroxidases
    • Dunford, H.B.1
  • 7
    • 0036670771 scopus 로고    scopus 로고
    • Toxicity of myoglobin and haemoglobin: Oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage
    • Reeder, B. J., Sharpe, M. A., Kay, A. D., Kerr, M., Moore, K. and Wilson, M. T. (2002) Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage. Biochem. Soc. Trans. 30, 745-748
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 745-748
    • Reeder, B.J.1    Sharpe, M.A.2    Kay, A.D.3    Kerr, M.4    Moore, K.5    Wilson, M.T.6
  • 8
    • 7244243910 scopus 로고    scopus 로고
    • Reeder, B. J., Svistunenko, D. A., Cooper, C. E. and Wilson, M. T. (2004) The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxid. Redox Signalling 6, 954-966
    • Reeder, B. J., Svistunenko, D. A., Cooper, C. E. and Wilson, M. T. (2004) The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxid. Redox Signalling 6, 954-966
  • 10
    • 33645846958 scopus 로고    scopus 로고
    • Resonance Raman spectroscopy of oxoiron(IV) porphyrin p-cation radical and oxoiron(IV) hemes in peroxidase intermediates
    • Terner, J., Palaniappan, V., Gold, A., Weiss, R., Fitzgerald, M. M., Sullivan, A. M. and Hosten, C. M. (2006) Resonance Raman spectroscopy of oxoiron(IV) porphyrin p-cation radical and oxoiron(IV) hemes in peroxidase intermediates. J. Inorg. Biochem. 100, 480-501
    • (2006) J. Inorg. Biochem , vol.100 , pp. 480-501
    • Terner, J.1    Palaniappan, V.2    Gold, A.3    Weiss, R.4    Fitzgerald, M.M.5    Sullivan, A.M.6    Hosten, C.M.7
  • 12
    • 33645879244 scopus 로고    scopus 로고
    • Stalking intermediates in oxygen activation by iron enzymes: Motivation and method
    • Bollinger, Jr, J. M. and Krebs, C. (2006) Stalking intermediates in oxygen activation by iron enzymes: motivation and method. J. Inorg. Biochem. 100, 586-605
    • (2006) J. Inorg. Biochem , vol.100 , pp. 586-605
    • Bollinger Jr, J.M.1    Krebs, C.2
  • 13
    • 33645856788 scopus 로고    scopus 로고
    • On the status of ferryl protonation
    • Behan, R. K. and Green, M. T. (2006) On the status of ferryl protonation. J. Inorg. Biochem. 100, 448-459
    • (2006) J. Inorg. Biochem , vol.100 , pp. 448-459
    • Behan, R.K.1    Green, M.T.2
  • 14
    • 0036941303 scopus 로고    scopus 로고
    • An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2
    • Hersleth, H. P., Dalhus, B., Gorbitz, C. H. and Andersson, K. K. (2002) An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2. J. Biol. Inorg. Chem. 7, 299-304
    • (2002) J. Biol. Inorg. Chem , vol.7 , pp. 299-304
    • Hersleth, H.P.1    Dalhus, B.2    Gorbitz, C.H.3    Andersson, K.K.4
  • 16
    • 0018169213 scopus 로고
    • Heme-linked ionization in compounds I and II of horseradish peroxidases A2 and C
    • Hayashi, Y. and Yamazaki, I. (1978) Heme-linked ionization in compounds I and II of horseradish peroxidases A2 and C. Arch. Biochem. Biophys. 190, 446-453
    • (1978) Arch. Biochem. Biophys , vol.190 , pp. 446-453
    • Hayashi, Y.1    Yamazaki, I.2
  • 17
    • 2942679678 scopus 로고    scopus 로고
    • Oxoiron(IV) in chloroperoxidase compound II is basic: Implications for P450 chemistry
    • Green, M. T., Dawson, J. H. and Gray, H. B. (2004) Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry. Science 304, 1653-1656
    • (2004) Science , vol.304 , pp. 1653-1656
    • Green, M.T.1    Dawson, J.H.2    Gray, H.B.3
  • 18
    • 28044448295 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry
    • Stone, K. L., Behan, R. K. and Green, M. T. (2005) X-ray absorption spectroscopy of chloroperoxidase compound I: insight into the reactive intermediate of P450 chemistry. Proc. Natl. Acad. Sci. U.S.A. 102, 16563-16565
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 16563-16565
    • Stone, K.L.1    Behan, R.K.2    Green, M.T.3
  • 19
    • 33646498740 scopus 로고    scopus 로고
    • Evidence for two ferryl species in chloroperoxidase compound II
    • Stone, K. L., Hoffart, L. M., Behan, R. K., Krebs, C. and Green, M. T. (2006) Evidence for two ferryl species in chloroperoxidase compound II. J. Am. Chem. Soc. 128, 6147-6153
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 6147-6153
    • Stone, K.L.1    Hoffart, L.M.2    Behan, R.K.3    Krebs, C.4    Green, M.T.5
  • 20
    • 33244476516 scopus 로고    scopus 로고
    • Application of Badger's rule to heme and non-heme iron-oxygen bonds: An examination of ferryl protonation states
    • Green, M. T. (2006) Application of Badger's rule to heme and non-heme iron-oxygen bonds: an examination of ferryl protonation states. J. Am. Chem. Soc. 128, 1902-1906
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 1902-1906
    • Green, M.T.1
  • 21
    • 33747616214 scopus 로고    scopus 로고
    • Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide
    • Stone, K. L., Behan, R. K. and Green, M. T. (2006) Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide. Proc. Natl. Acad. Sci. U.S.A. 103, 12307-12310
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 12307-12310
    • Stone, K.L.1    Behan, R.K.2    Green, M.T.3
  • 23
    • 20444466524 scopus 로고    scopus 로고
    • Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: What have we learned?
    • Smulevich, G., Feis, A. and Howes, B. D. (2005) Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned? Acc. Chem. Res. 38, 433-440
    • (2005) Acc. Chem. Res , vol.38 , pp. 433-440
    • Smulevich, G.1    Feis, A.2    Howes, B.D.3
  • 24
    • 33646471517 scopus 로고    scopus 로고
    • Mössbauer identification of a protonated ferryl species in catalase from Proteus mirabilis: Density functional calculations on related models
    • Horner, O., Oddou, J. L., Mouesca, J. M. and Jouve, H. M. (2006) Mössbauer identification of a protonated ferryl species in catalase from Proteus mirabilis: density functional calculations on related models. J. Inorg. Biochem. 100, 477-479
    • (2006) J. Inorg. Biochem , vol.100 , pp. 477-479
    • Horner, O.1    Oddou, J.L.2    Mouesca, J.M.3    Jouve, H.M.4
  • 25
    • 13844255406 scopus 로고    scopus 로고
    • Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view
    • Svistunenko, D. A. (2005) Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view. Biochim. Biophys. Acta 1707, 127-155
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 127-155
    • Svistunenko, D.A.1
  • 26
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • Kelso King, N. and Winfield, M. E. (1963) The mechanism of metmyoglobin oxidation. J. Biol. Chem. 238, 1520-1528
    • (1963) J. Biol. Chem , vol.238 , pp. 1520-1528
    • Kelso King, N.1    Winfield, M.E.2
  • 28
    • 0035371323 scopus 로고    scopus 로고
    • The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species
    • Reeder, B. J. and Wilson, M. T. (2001) The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species. Free Radical Biol. Med. 30, 1311-1318
    • (2001) Free Radical Biol. Med , vol.30 , pp. 1311-1318
    • Reeder, B.J.1    Wilson, M.T.2
  • 29
    • 0037039353 scopus 로고    scopus 로고
    • Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin
    • Reeder, B. J., Svistunenko, D. A., Sharpe, M. A. and Wilson, M. T. (2002) Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin. Biochemistry 41, 367-375
    • (2002) Biochemistry , vol.41 , pp. 367-375
    • Reeder, B.J.1    Svistunenko, D.A.2    Sharpe, M.A.3    Wilson, M.T.4
  • 30
    • 0032521652 scopus 로고    scopus 로고
    • Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid
    • Reeder, B. J. and Wilson, M. T. (1998) Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid. Biochem. J. 330, 1317-1323
    • (1998) Biochem. J , vol.330 , pp. 1317-1323
    • Reeder, B.J.1    Wilson, M.T.2
  • 31
    • 0036304241 scopus 로고    scopus 로고
    • Role of histidine 42 in ascorbate peroxidase: Kinetic analysis of the H42A and H42E variants
    • Lad, L., Mewies, M., Basran, J., Scrutton, N. S. and Raven, E. L. (2002) Role of histidine 42 in ascorbate peroxidase: kinetic analysis of the H42A and H42E variants. Eur. J. Biochem. 269, 3182-3192
    • (2002) Eur. J. Biochem , vol.269 , pp. 3182-3192
    • Lad, L.1    Mewies, M.2    Basran, J.3    Scrutton, N.S.4    Raven, E.L.5
  • 32
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. (1993) Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98, 5648
    • (1993) J. Chem. Phys , vol.98 , pp. 5648
    • Becke, A.D.1
  • 33
    • 5944261746 scopus 로고    scopus 로고
    • Perdew, J. P. (1986) Density-functional approximation for the correlation energy of the inhomogeneous electron gas. Condens. Matter Mater. Phys. Rev. B 33, 8822-8824
    • Perdew, J. P. (1986) Density-functional approximation for the correlation energy of the inhomogeneous electron gas. Condens. Matter Mater. Phys. Rev. B 33, 8822-8824
  • 34
    • 27744527982 scopus 로고    scopus 로고
    • Transient species involved in catalytic dioxygen/peroxide activation by hemoproteins: Possible involvement of protonated Compound I species
    • Silaghi-Dumitrescu, R. and Cooper, C. E. (2005) Transient species involved in catalytic dioxygen/peroxide activation by hemoproteins: possible involvement of protonated Compound I species. Dalton Trans. 3477-3482
    • (2005) Dalton Trans , pp. 3477-3482
    • Silaghi-Dumitrescu, R.1    Cooper, C.E.2
  • 36
    • 0033800107 scopus 로고    scopus 로고
    • Decreasing mortality with primary percutaneous coronary intervention in patients with acute myocardial infarction: The Mayo Clinic experience from 1991 through 1997
    • Velianou, J. L., Wilson, S. H., Reeder, G. S., Caplice, N. M., Grill, D. E., Holmes, Jr, D. R. and Bell, M. R. (2000) Decreasing mortality with primary percutaneous coronary intervention in patients with acute myocardial infarction: the Mayo Clinic experience from 1991 through 1997. Mayo Clin. Proc. 75, 994-1001
    • (2000) Mayo Clin. Proc , vol.75 , pp. 994-1001
    • Velianou, J.L.1    Wilson, S.H.2    Reeder, G.S.3    Caplice, N.M.4    Grill, D.E.5    Holmes Jr, D.R.6    Bell, M.R.7
  • 38
    • 0033610847 scopus 로고    scopus 로고
    • A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure
    • Moore, K. P., Holt, S. G., Patel, R. P., Svistunenko, D. A., Zackert, W., Goodier, D., Reeder, B. J., Clozel, M., Anand, R. et al. (1998) A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure. J. Biol. Chem. 273, 31731-31737
    • (1998) J. Biol. Chem , vol.273 , pp. 31731-31737
    • Moore, K.P.1    Holt, S.G.2    Patel, R.P.3    Svistunenko, D.A.4    Zackert, W.5    Goodier, D.6    Reeder, B.J.7    Clozel, M.8    Anand, R.9
  • 39
    • 27744494382 scopus 로고    scopus 로고
    • On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide
    • Cooper, C. E., Jurd, M., Nicholls, P., Wankasi, M. M., Svistunenko, D. A., Reeder, B. J. and Wilson, M. T. (2005) On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide. Dalton Trans. 3483-3488
    • (2005) Dalton Trans , pp. 3483-3488
    • Cooper, C.E.1    Jurd, M.2    Nicholls, P.3    Wankasi, M.M.4    Svistunenko, D.A.5    Reeder, B.J.6    Wilson, M.T.7
  • 40
    • 0019787519 scopus 로고
    • Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: A hypothesis
    • Ames, B. N., Cathcart, R., Schwlers, E. and Hochstein, P. (1981) Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis. Proc. Natl. Acad. Sci. U.S.A. 78, 6858-6862
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwlers, E.3    Hochstein, P.4
  • 41
    • 0001218860 scopus 로고
    • Ascorbate is an outstanding antioxidant in human blood plasma
    • Frei, B., England, L. and Ames, B. N. (1989) Ascorbate is an outstanding antioxidant in human blood plasma. Proc. Natl. Acad. Sci. U.S.A. 86, 6377-6381
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 6377-6381
    • Frei, B.1    England, L.2    Ames, B.N.3
  • 43
    • 0343550480 scopus 로고    scopus 로고
    • Protein binding in deactivation of ferrylmyoglobin by chlorogenate and ascorbate
    • Carlsen, C. U., Kroger-Ohlsen, M. V., Bellio, R. and Skibsted, L. H. (2000) Protein binding in deactivation of ferrylmyoglobin by chlorogenate and ascorbate. J. Agric. Food Chem. 48, 204-212
    • (2000) J. Agric. Food Chem , vol.48 , pp. 204-212
    • Carlsen, C.U.1    Kroger-Ohlsen, M.V.2    Bellio, R.3    Skibsted, L.H.4
  • 44
    • 0024348254 scopus 로고
    • pH-dependent forms of the ferryl haem in myoglobin peroxide analysed by variable-temperature magnetic circular dichroism
    • Foote, N., Gadsby, P. M. A., Greenwood, C. and Thomson, A. J. (1989) pH-dependent forms of the ferryl haem in myoglobin peroxide analysed by variable-temperature magnetic circular dichroism. Biochem. J. 261, 515-522
    • (1989) Biochem. J , vol.261 , pp. 515-522
    • Foote, N.1    Gadsby, P.M.A.2    Greenwood, C.3    Thomson, A.J.4
  • 45
    • 0001459583 scopus 로고
    • Hemoglobin and myoglobin in their reactions with ligands
    • Neuberger, A. and Tatum, E. L, eds, pp, North-Holland Publishing Company, Amsterdam and London
    • Antonini, E. and Brunori, M. (1971) Hemoglobin and myoglobin in their reactions with ligands. In Frontiers in Biology (Neuberger, A. and Tatum, E. L., eds.), pp. 1-52, North-Holland Publishing Company, Amsterdam and London
    • (1971) Frontiers in Biology , pp. 1-52
    • Antonini, E.1    Brunori, M.2


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