메뉴 건너뛰기




Volumn 40, Issue 1, 2006, Pages 67-74

Non-oxygen-forming pathways of hydrogen peroxide degradation by bovine liver catalase at low hydrogen peroxide fluxes

Author keywords

Catalase; Compound I; Compound II; Hydrogen peroxide; Metabolism; NADPH; Reductive

Indexed keywords

CATALASE; HYDROGEN PEROXIDE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 29744468218     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.1080/10715760500381029     Document Type: Article
Times cited : (18)

References (24)
  • 1
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita, I and Rossmann, MG. (1985) The active center of catalase J Mol Biol, 185, pp. 21 - 37.
    • (1985) J Mol Biol , vol.185 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 2
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam, CD Arvai, AS Bourne, Y and Tainer, JA. (2000) Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism J Mol Biol, 296, pp. 295 - 309.
    • (2000) J Mol Biol , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 3
    • 0038360689 scopus 로고    scopus 로고
    • Understanding the structure and function of catalases: Clues from molecular evolution and in vitro mutagenesis
    • Zamocky, M and Koller, F. (1999) Understanding the structure and function of catalases: Clues from molecular evolution and in vitro mutagenesis Prog Biophys Mol Biol, 72, pp. 19 - 66.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 19-66
    • Zamocky, M.1    Koller, F.2
  • 4
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B Sies, H and Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs Physiol Rev, 59, pp. 527 - 605.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 5
    • 0000179774 scopus 로고
    • The reactions of catalase in the presence of the notatin system
    • Chance, B. (1950) The reactions of catalase in the presence of the notatin system J Biochem, 46, pp. 387 - 402.
    • (1950) J Biochem , vol.46 , pp. 387-402
    • Chance, B.1
  • 6
    • 0029266693 scopus 로고
    • Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide
    • Lardinois, OM. (1995) Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide Free Radic Res, 22, pp. 251 - 274.
    • (1995) Free Radic Res , vol.22 , pp. 251-274
    • Lardinois, O.M.1
  • 7
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH: Kinetics and stoichiometry
    • Kirkman, HN Rolfo, M Ferraris, AM and Gaetani, GF. (1999) Mechanisms of protection of catalase by NADPH: Kinetics and stoichiometry J Biol Chem, 274, pp. 13908 - 13914.
    • (1999) J Biol Chem , vol.274 , pp. 13908-13914
    • Kirkman, H.N.1    Rolfo, M.2    Ferraris, A.M.3    Gaetani, G.F.4
  • 8
    • 0028364445 scopus 로고
    • NADPH binding and control of catalase compound II formation: Comparison of bovine, yeast, and Escherichia coli enzymes
    • Hillar, A Nicholls, P Switala, J and Loewen, PC. (1994) NADPH binding and control of catalase compound II formation: Comparison of bovine, yeast, and Escherichia coli enzymes Biochem J, 300, pp. 531 - 539.
    • (1994) Biochem J , vol.300 , pp. 531-539
    • Hillar, A.1    Nicholls, P.2    Switala, J.3    Loewen, P.C.4
  • 9
    • 0026470233 scopus 로고
    • A mechanism for NADPH inhibition of catalase compound II formation
    • Hillar, A and Nicholls, P. (1992) A mechanism for NADPH inhibition of catalase compound II formation FEBS Lett, 314, pp. 179 - 182.
    • (1992) FEBS Lett , vol.314 , pp. 179-182
    • Hillar, A.1    Nicholls, P.2
  • 10
    • 0000286714 scopus 로고
    • Mechanism of one-electron oxidation of NAD(P)H and function of NADPH bound to catalase
    • Almarsson, Ö Sinha, A Gopinath, E and Bruice, TC. (1993) Mechanism of one-electron oxidation of NAD(P)H and function of NADPH bound to catalase J Am Chem Soc, 115, pp. 7093 - 7102.
    • (1993) J Am Chem Soc , vol.115 , pp. 7093-7102
    • Almarsson, Ö.1    Sinha, A.2    Gopinath, E.3    Bruice, T.C.4
  • 11
    • 0035856548 scopus 로고    scopus 로고
    • Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity
    • Andreoletti, P Gambarelli, S Sainz, G Stojanoff, V White, C Desfonds, G Gagnon, J Gaillard, J and Jouve, HM. (2001) Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity Biochemistry, 40, pp. 13734 - 13743.
    • (2001) Biochemistry , vol.40 , pp. 13734-13743
    • Andreoletti, P.1    Gambarelli, S.2    Sainz, G.3    Stojanoff, V.4    White, C.5    Desfonds, G.6    Gagnon, J.7    Gaillard, J.8    Jouve, H.M.9
  • 12
    • 13444257622 scopus 로고    scopus 로고
    • A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase
    • Gaetani, GF Ferraris, AM Sanna, P and Kirkman, HN. (2005) A novel NADPH:(Bound) NADP+ reductaBe and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase Biochem J, 385, pp. 763 - 768.
    • (2005) Biochem J , vol.385 , pp. 763-768
    • Gaetani, G.F.1    Ferraris, A.M.2    Sanna, P.3    Kirkman, H.N.4
  • 13
    • 0023094372 scopus 로고
    • The function of catalase-bound NADPH
    • Kirkman, HN Galiano, S and Gaetani, GF. (1987) The function of catalase-bound NADPH J Biol Chem, 262, pp. 660 - 666.
    • (1987) J Biol Chem , vol.262 , pp. 660-666
    • Kirkman, H.N.1    Galiano, S.2    Gaetani, G.F.3
  • 14
    • 0001113307 scopus 로고
    • The enzyme-substrate compounds of bacterial catalase and peroxides
    • Chance, B and Herbert, D. (1950) The enzyme-substrate compounds of bacterial catalase and peroxides Biochem J, 46, pp. 402 - 414.
    • (1950) Biochem J , vol.46 , pp. 402-414
    • Chance, B.1    Herbert, D.2
  • 15
    • 0000024076 scopus 로고
    • Catalase
    • Weinheim: Verlag Chemie
    • Aebi, HE.(1983) Catalase. In Methods of enzymatic analysis. (pp. 273 - 286).Weinheim: Verlag Chemie.
    • (1983) Methods of Enzymatic Analysis , pp. 273-286
    • Aebi, H.E.1
  • 17
    • 0001408791 scopus 로고
    • Catalases
    • New York: Academic Press
    • Nicholls, P and Schonbaum, GR.(1963) Catalases. In The enzymes. (pp. 147 - 225).New York: Academic Press.
    • (1963) The Enzymes , pp. 147-225
    • Nicholls, P.1    Schonbaum, G.R.2
  • 18
    • 0000685339 scopus 로고
    • The spectra of the enzyme-substrate complexes of catalase and peroxidase
    • Chance, B. (1952) The spectra of the enzyme-substrate complexes of catalase and peroxidase Arch Biochem Biophys, 41, pp. 404 - 415.
    • (1952) Arch Biochem Biophys , vol.41 , pp. 404-415
    • Chance, B.1
  • 19
    • 0030835382 scopus 로고    scopus 로고
    • EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: Formation of porphyrin and tyrosyl radical intermediates
    • Ivancich, A Jouve, HM Sartor, B and Gaillard, J. (1997) EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: Formation of porphyrin and tyrosyl radical intermediates Biochemistry, 36, pp. 9356 - 9364.
    • (1997) Biochemistry , vol.36 , pp. 9356-9364
    • Ivancich, A.1    Jouve, H.M.2    Sartor, B.3    Gaillard, J.4
  • 20
    • 0029089392 scopus 로고
    • Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR
    • Bicout, DJ Field, MJ Gouet, P and Jouve, HM. (1995) Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR Biochim Biophys Acta, 1252, pp. 172 - 176.
    • (1995) Biochim Biophys Acta , vol.1252 , pp. 172-176
    • Bicout, D.J.1    Field, M.J.2    Gouet, P.3    Jouve, H.M.4
  • 21
    • 0029059057 scopus 로고
    • Electron tunneling and ab initio calculations related to the one-electron oxidation of NAD(P)H bound to catalase
    • Olson, LP and Bruice, TC. (1995) Electron tunneling and ab initio calculations related to the one-electron oxidation of NAD(P)H bound to catalase Biochemistry, 34, pp. 7335 - 7347.
    • (1995) Biochemistry , vol.34 , pp. 7335-7347
    • Olson, L.P.1    Bruice, T.C.2
  • 22
    • 14844321894 scopus 로고    scopus 로고
    • Functional and structural analysis of catalase oxidized by singlet oxygen
    • Diaz, A Munoz-Clares, RA Rangel, P Valdes, VJ and Hansberg, W. (2005) Functional and structural analysis of catalase oxidized by singlet oxygen Biochimie, 87, pp. 205 - 214.
    • (2005) Biochimie , vol.87 , pp. 205-214
    • Diaz, A.1    Munoz-Clares, R.A.2    Rangel, P.3    Valdes, V.J.4    Hansberg, W.5
  • 23
    • 2642617823 scopus 로고    scopus 로고
    • Oxidation of catalase by singlet oxygen
    • Lledias, F Rangel, P and Hansberg, W. (1998) Oxidation of catalase by singlet oxygen J Biol Chem, 273, pp. 10630 - 10637.
    • (1998) J Biol Chem , vol.273 , pp. 10630-10637
    • Lledias, F.1    Rangel, P.2    Hansberg, W.3
  • 24
    • 0023039125 scopus 로고
    • NADP-binding proteins causing reduced availability and sigmoid release of NADP+ in human erythrocytes
    • Kirkman, HN Gaetani, GF and Clemons, EH. (1986) NADP-binding proteins causing reduced availability and sigmoid release of NADP+ in human erythrocytes J Biol Chem, 261, pp. 4039 - 4045.
    • (1986) J Biol Chem , vol.261 , pp. 4039-4045
    • Kirkman, H.N.1    Gaetani, G.F.2    Clemons, E.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.