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Volumn 46, Issue 1, 2007, Pages 11-22

Relationship between the size of the bottleneck 15 Å from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CATALASE; FORMATION RATE; REACTIVE INTERMEDIATES;

EID: 33846110459     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061519w     Document Type: Article
Times cited : (45)

References (69)
  • 1
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H., and Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs, Physiol. Rev. 59, 527-605.
    • (1979) Physiol. Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 2
    • 77956932249 scopus 로고
    • Catalase
    • Boyer, P. D, Ed, pp, Academic Press, New York
    • Schonbaum, G. R., and Chance, B. (1976) Catalase, in The enzymes (Boyer, P. D., Ed.) pp 363-408, Academic Press, New York.
    • (1976) The enzymes , pp. 363-408
    • Schonbaum, G.R.1    Chance, B.2
  • 3
    • 0014819568 scopus 로고
    • Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role
    • Deisseroth, A., and Dounce, A. L. (1970) Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role, Physiol. Rev. 50, 319-375.
    • (1970) Physiol. Rev , vol.50 , pp. 319-375
    • Deisseroth, A.1    Dounce, A.L.2
  • 4
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita, I., and Rossmann, M. G. (1985) The active center of catalase, J. Mol. Biol. 185, 21-37.
    • (1985) J. Mol. Biol , vol.185 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 5
    • 0029001848 scopus 로고
    • Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH
    • Gouet, P., Jouve, H. M., and Dideberg, O. (1995) Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH, J. Mol. Biol. 249, 933-954.
    • (1995) J. Mol. Biol , vol.249 , pp. 933-954
    • Gouet, P.1    Jouve, H.M.2    Dideberg, O.3
  • 7
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam, C. D., Arvai, A. S., Bourne, Y., and Tainer, J. A. (2000) Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism, J. Mol. Blol. 296, 295-309.
    • (2000) J. Mol. Blol , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 9
    • 0029020576 scopus 로고
    • Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity
    • Zamocky, M., Herzog, C., Nykyri, L. M., and Koller, F. (1995) Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity, FEBS Lett. 367, 241-245.
    • (1995) FEBS Lett , vol.367 , pp. 241-245
    • Zamocky, M.1    Herzog, C.2    Nykyri, L.M.3    Koller, F.4
  • 10
    • 0043234246 scopus 로고    scopus 로고
    • An electrical potential in the access channel of catalases enhances catalysis
    • Chelikani, P., Carpena, X., Fita, I., and Loewen, P. C. (2003) An electrical potential in the access channel of catalases enhances catalysis, J. Biol. Chem. 278, 31290-31296.
    • (2003) J. Biol. Chem , vol.278 , pp. 31290-31296
    • Chelikani, P.1    Carpena, X.2    Fita, I.3    Loewen, P.C.4
  • 11
    • 0018367454 scopus 로고
    • Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities
    • Claiborne, A., and Fridovich, I. (1979) Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities, J. Biol. Chem. 254, 4245-4252.
    • (1979) J. Biol. Chem , vol.254 , pp. 4245-4252
    • Claiborne, A.1    Fridovich, I.2
  • 12
    • 0023654802 scopus 로고
    • Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata
    • Hochman, A., and Shemesh, A. (1987) Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata, J. Biol. Chem. 262, 6871-6876.
    • (1987) J. Biol. Chem , vol.262 , pp. 6871-6876
    • Hochman, A.1    Shemesh, A.2
  • 13
    • 0021111935 scopus 로고
    • Isolation and characterization of the pseudocatalase of Lactobacillus plantarum
    • Kono, Y., and Fridovich, I. (1983) Isolation and characterization of the pseudocatalase of Lactobacillus plantarum, J. Biol. Chem. 258, 6015-6019.
    • (1983) J. Biol. Chem , vol.258 , pp. 6015-6019
    • Kono, Y.1    Fridovich, I.2
  • 14
    • 0023007996 scopus 로고
    • Characterization of a manganese-containing catalase from the obligate thermophile Thermoleophilum album
    • Allgood, G. S., and Perry, J. J. (1986) Characterization of a manganese-containing catalase from the obligate thermophile Thermoleophilum album, J. Bacteriol. 168, 563-567.
    • (1986) J. Bacteriol , vol.168 , pp. 563-567
    • Allgood, G.S.1    Perry, J.J.2
  • 15
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz, M. G., Klassen, G. R., and Loewen, P. C. (1997) Phylogenetic relationships among prokaryotic and eukaryotic catalases, Mol. Biol. Evol. 14, 951-958.
    • (1997) Mol. Biol. Evol , vol.14 , pp. 951-958
    • Klotz, M.G.1    Klassen, G.R.2    Loewen, P.C.3
  • 16
    • 35448998145 scopus 로고    scopus 로고
    • Enzymology and structure of catalases
    • Nicholls, P., Fita, I., and Loewen, P. C. (2001) Enzymology and structure of catalases, Adv. Inorg. Chem. 51, 51-106.
    • (2001) Adv. Inorg. Chem , vol.51 , pp. 51-106
    • Nicholls, P.1    Fita, I.2    Loewen, P.C.3
  • 17
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structure and properties among catalases
    • Chelikani, P., Fita, I., and Loewen, P. C. (2004) Diversity of structure and properties among catalases, Cell. Mol. Life Sci. 61, 192-208.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 26
    • 16644362979 scopus 로고    scopus 로고
    • The three-dimensional structure of catalase from Enterococcus faecalis
    • Hakansson, K. O., Brugna, M., and Tasse, L. (2004) The three-dimensional structure of catalase from Enterococcus faecalis, Acta Crystallogr. D60, 1374-1380.
    • (2004) Acta Crystallogr , vol.D60 , pp. 1374-1380
    • Hakansson, K.O.1    Brugna, M.2    Tasse, L.3
  • 27
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr, S. B., and Kogoma, T. (1991) Oxidative stress responses in Escherichia coli and Salmonella typhimurium, Microbiol. Rev. 55, 561-585.
    • (1991) Microbiol. Rev , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 29
    • 0034319164 scopus 로고    scopus 로고
    • Gene cloning and expression of the catalase from the hydrogen peroxide-resistant bacterium Vibrio rumoiensis S-1 and its subcellular localization
    • Ichise, N., Morita, N., Kawasaki, K., Yumoto, I., and Okuyama, H. (2000) Gene cloning and expression of the catalase from the hydrogen peroxide-resistant bacterium Vibrio rumoiensis S-1 and its subcellular localization, J. Biosci. Bioeng. 90, 530-534.
    • (2000) J. Biosci. Bioeng , vol.90 , pp. 530-534
    • Ichise, N.1    Morita, N.2    Kawasaki, K.3    Yumoto, I.4    Okuyama, H.5
  • 31
    • 0000561773 scopus 로고    scopus 로고
    • Henry's law constant determinations for hydrogen peroxide, methyl hydroperoxide, hydroxymethyl hydroperoxide, ethyl hydroperoxide, and peroxyacetic acid
    • O'Sullivan, D. W., Lee, M. Y., Noone, B. C., and Heikes, B. G. (1996) Henry's law constant determinations for hydrogen peroxide, methyl hydroperoxide, hydroxymethyl hydroperoxide, ethyl hydroperoxide, and peroxyacetic acid, J. Phys. Chem. 100, 3241-3247.
    • (1996) J. Phys. Chem , vol.100 , pp. 3241-3247
    • O'Sullivan, D.W.1    Lee, M.Y.2    Noone, B.C.3    Heikes, B.G.4
  • 32
    • 0034728303 scopus 로고    scopus 로고
    • Computational and experimental studies of chemical ionization mass spectrometric detection techniques for atmospherically relevant peroxides
    • Messer, B. M., Stielstra, D. E., Cappa, C. D., Scholtens, K. W., and Elrod, M. J. (2000) Computational and experimental studies of chemical ionization mass spectrometric detection techniques for atmospherically relevant peroxides, Int. J. Mass Spectrom. 197, 219-235.
    • (2000) Int. J. Mass Spectrom , vol.197 , pp. 219-235
    • Messer, B.M.1    Stielstra, D.E.2    Cappa, C.D.3    Scholtens, K.W.4    Elrod, M.J.5
  • 33
    • 0015422147 scopus 로고
    • Formation of compound I by the reaction of catalase with peroxoacetic acid
    • Jones, P., and Middlemiss, D. N. (1972) Formation of compound I by the reaction of catalase with peroxoacetic acid, Biochem. J. 130, 411-415.
    • (1972) Biochem. J , vol.130 , pp. 411-415
    • Jones, P.1    Middlemiss, D.N.2
  • 34
    • 0001060636 scopus 로고
    • Thermodynamics of iodine solubility and triiodide ion formation in water and in deuterium oxide
    • Ramette, R. W., and Sandford, R. W. (1965) Thermodynamics of iodine solubility and triiodide ion formation in water and in deuterium oxide, J. Am. Chem. Soc. 87, 5001-5005.
    • (1965) J. Am. Chem. Soc , vol.87 , pp. 5001-5005
    • Ramette, R.W.1    Sandford, R.W.2
  • 35
    • 0014515230 scopus 로고
    • Electron paramagnetic resonance study of bovine liver catalase
    • Torii, K., and Ogura, Y. (1969) Electron paramagnetic resonance study of bovine liver catalase, J. Biochem. 65, 825-827.
    • (1969) J. Biochem , vol.65 , pp. 825-827
    • Torii, K.1    Ogura, Y.2
  • 36
    • 0001177754 scopus 로고
    • Reconstitution of acid-denatured catalase
    • Samejima, T., and Yang, J. T. (1963) Reconstitution of acid-denatured catalase, J. Biol. Chem. 238, 3256-3261.
    • (1963) J. Biol. Chem , vol.238 , pp. 3256-3261
    • Samejima, T.1    Yang, J.T.2
  • 37
    • 0014796962 scopus 로고
    • Dissociation of catalase. A correlation between changes in sedimentation and spectroscopic properties accompanying dissociation of bacterial catalase in alkaline solution
    • Jones, P., Pain, R. H., and Suggett, A. (1970) Dissociation of catalase. A correlation between changes in sedimentation and spectroscopic properties accompanying dissociation of bacterial catalase in alkaline solution, Biochem. J. 118, 319-323.
    • (1970) Biochem. J , vol.118 , pp. 319-323
    • Jones, P.1    Pain, R.H.2    Suggett, A.3
  • 38
    • 10644232178 scopus 로고
    • Primary compounds of catalase and peroxidase
    • Brill, A. S., and Williams, R. J. P. (1961) Primary compounds of catalase and peroxidase, Biochem. J. 78, 253-262.
    • (1961) Biochem. J , vol.78 , pp. 253-262
    • Brill, A.S.1    Williams, R.J.P.2
  • 40
    • 0006739227 scopus 로고
    • Spectrophotometric. method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle
    • De Duve, C. A. (1948) Spectrophotometric. method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle, Acta Chem. Scand. 2, 264-289.
    • (1948) Acta Chem. Scand , vol.2 , pp. 264-289
    • De Duve, C.A.1
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 0016701378 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes
    • Hildebraunt, A. G., and Roots, I. (1975) Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes, Arch. Biochem. Biophys. 171, 385-397.
    • (1975) Arch. Biochem. Biophys , vol.171 , pp. 385-397
    • Hildebraunt, A.G.1    Roots, I.2
  • 43
    • 0001423896 scopus 로고
    • Effect of pH upon the reaction kinetics of the enzyme-substrate compounds of catalase
    • Chance, B. (1952) Effect of pH upon the reaction kinetics of the enzyme-substrate compounds of catalase, J. Biol. Chem. 194, 471-481.
    • (1952) J. Biol. Chem , vol.194 , pp. 471-481
    • Chance, B.1
  • 44
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur, J. (1961) A procedure for the isolation of deoxyribonucleic acid from micro-organisms, J. Mol. Biol. 3, 208-218.
    • (1961) J. Mol. Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 45
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., Gerber, A. S., and Hartl, D. L. (1988) Genetic applications of an inverse polymerase chain reaction, Genetics 120, 621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 46
    • 0025913445 scopus 로고
    • Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium
    • Jancarik, J., Scott, W. G., Milligan, D. L., Koshland, D. E., Jr., and Kim, S. H. (1991) Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium, J. Mol. Biol. 221, 31-34.
    • (1991) J. Mol. Biol , vol.221 , pp. 31-34
    • Jancarik, J.1    Scott, W.G.2    Milligan, D.L.3    Koshland Jr., D.E.4    Kim, S.H.5
  • 47
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson, A. (1990) Current approaches to macromolecular crystallization, Eur. J. Biochem. 189, 1-23.
    • (1990) Eur. J. Biochem , vol.189 , pp. 1-23
    • McPherson, A.1
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 0000560808 scopus 로고    scopus 로고
    • Molrep: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997) Molrep: An automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
    • (1997) J. Appl. Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 50
    • 0345345539 scopus 로고
    • The NADPH binding site on beef liver catalase
    • Fita, I., and Rossmann, M. G. (1985) The NADPH binding site on beef liver catalase, Proc. Natl. Acad. Sci. U.S.A. 82, 1604-1608.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 1604-1608
    • Fita, I.1    Rossmann, M.G.2
  • 52
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 53
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal-structures
    • Brunger, A. T. (1992) Free R-value: A novel statistical quantity for assessing the accuracy of crystal-structures, Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 54
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 55
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams, M. A., Goodfellow, J. M., and Thornton, J. M. (1994) Buried waters and internal cavities in monomeric proteins, Protein Sci. 3, 1224-1235.
    • (1994) Protein Sci , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 56
    • 0018763006 scopus 로고
    • Spectral studies of human erythrocyte catalase
    • Palcic, M., and Dunford, H. B. (1979) Spectral studies of human erythrocyte catalase, Can. J. Biochem. 57, 321-329.
    • (1979) Can. J. Biochem , vol.57 , pp. 321-329
    • Palcic, M.1    Dunford, H.B.2
  • 57
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968) Solvent content of protein crystals, J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 58
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R. A., and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein-structure refinement, Acta Crystallogr. A47, 392-400.
    • (1991) Acta Crystallogr , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 60
    • 0038752613 scopus 로고    scopus 로고
    • Read, T. D, Peterson, S. N, Tourasse, N, Baillie, L. W, Paulsen, I. T, Nelson, K. E, Tettelin, H, Fouts, D. E, Eisen, J. A, Gill, S. R, Holtzapple, E. K, Okstad, O. A, Helgason, E, Rilstone, J, Wu, M, Kolonay, J. F, Beanan, M. J, Dodson, R. J, Brinkac, L. M, Gwinn, M, DeBoy, R. T, Madpu, R, Daugherty, S. C, Durkin, A. S, Haft, D. H, Nelson, W. C, Peterson, J. D, Pop, M, Khouri, H. M, Radune, D, Benton, J. L, Mahamoud, Y, Jiang, L, Hance, I. R, Weidman, J. F, Berry, K. J, Plaut, R. D, Wolf, A. M, Watkins, K. L, Nierman, W. C, Hazen, A, Cline, R, Redmond, C, Thwaite, J. E, White, O, Salzberg, S. L, Thomason, B, Friedlander, A. M, Koehler, T. M, Hanna, P. C, Kolsto, A. B, and Fraser, C. M, 2003 The genome sequence of Bacillus anthracis ames and comparison to closely related bacteria, Nature 423, 81-86
    • Read, T. D., Peterson, S. N., Tourasse, N., Baillie, L. W., Paulsen, I. T., Nelson, K. E., Tettelin, H., Fouts, D. E., Eisen, J. A., Gill, S. R., Holtzapple, E. K., Okstad, O. A., Helgason, E., Rilstone, J., Wu, M., Kolonay, J. F., Beanan, M. J., Dodson, R. J., Brinkac, L. M., Gwinn, M., DeBoy, R. T., Madpu, R., Daugherty, S. C., Durkin, A. S., Haft, D. H., Nelson, W. C., Peterson, J. D., Pop, M., Khouri, H. M., Radune, D., Benton, J. L., Mahamoud, Y., Jiang, L., Hance, I. R., Weidman, J. F., Berry, K. J., Plaut, R. D., Wolf, A. M., Watkins, K. L., Nierman, W. C., Hazen, A., Cline, R., Redmond, C., Thwaite, J. E., White, O., Salzberg, S. L., Thomason, B., Friedlander, A. M., Koehler, T. M., Hanna, P. C., Kolsto, A. B., and Fraser, C. M. (2003) The genome sequence of Bacillus anthracis ames and comparison to closely related bacteria, Nature 423, 81-86.
  • 61
    • 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, 179-182.
    • (1992) FEBS Lett , vol.314 , pp. 179-182
    • Hillar, A.1    Nicholls, P.2
  • 62
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry
    • Kirkman, H. N., Rolfo, M., Ferraris, A. M., and Gaetani, G. F. (1999) Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry, J. Biol. Chem. 274, 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
  • 63
    • 0029059057 scopus 로고
    • Electron tunneling and ab initio calculations related to the one-electron oxidation of NAD(P)H bound to catalase
    • Olson, L. P., and Bruice, T. C. (1995) Electron tunneling and ab initio calculations related to the one-electron oxidation of NAD(P)H bound to catalase, Biochemistry 34, 7335-7347.
    • (1995) Biochemistry , vol.34 , pp. 7335-7347
    • Olson, L.P.1    Bruice, T.C.2
  • 64
    • 0000286714 scopus 로고
    • Mechanism of one-electron oxidation of NAD(P)H and function of NADPH bound to catalase
    • Almarsson, O., Sinha, A., Gopinath, E., and Bruice, T. C. (1993) Mechanism of one-electron oxidation of NAD(P)H and function of NADPH bound to catalase, J. Am. Chem. Soc. 115, 7093-7102.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 7093-7102
    • Almarsson, O.1    Sinha, A.2    Gopinath, E.3    Bruice, T.C.4
  • 65
    • 0030945035 scopus 로고    scopus 로고
    • Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli
    • Bravo, J., Fita, I., Ferrer, J. C., Ens, W., Hillar, A., Switala, J., and Loewen, P. C. (1997) Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli, Protein Sci. 6, 1016-1023.
    • (1997) Protein Sci , vol.6 , pp. 1016-1023
    • Bravo, J.1    Fita, I.2    Ferrer, J.C.3    Ens, W.4    Hillar, A.5    Switala, J.6    Loewen, P.C.7
  • 67
    • 0019321337 scopus 로고
    • The reaction of human erythrocyte catalase with hydroperoxides to form compound I
    • Palcic, M. M., and Dunford, H. B. (1980) The reaction of human erythrocyte catalase with hydroperoxides to form compound I, J. Biol. Chem. 255, 6128-6132.
    • (1980) J. Biol. Chem , vol.255 , pp. 6128-6132
    • Palcic, M.M.1    Dunford, H.B.2
  • 68
    • 0003514551 scopus 로고    scopus 로고
    • Wiley-VCH, New York
    • Dunford, H. B. (1999) Heme peroxidases, pp 435-453, Wiley-VCH, New York.
    • (1999) Heme peroxidases , pp. 435-453
    • Dunford, H.B.1
  • 69
    • 0037095620 scopus 로고    scopus 로고
    • Diversity of properties among catalases
    • Switala, J., and Loewen, P. C. (2002) Diversity of properties among catalases, Arch. Biochem. Biophys. 401, 145-154.
    • (2002) Arch. Biochem. Biophys , vol.401 , pp. 145-154
    • Switala, J.1    Loewen, P.C.2


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