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Volumn 52, Issue 7, 2013, Pages 1221-1226

Relative timing of hydrogen and proton transfers in the reaction of flavin oxidation catalyzed by choline oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCE SPECTROSCOPY; CHOLINE OXIDASE; FLAVIN OXIDATION; HYDROGEN AND PROTON TRANSFER; ISOTOPIC SUBSTITUTION; KINETIC ISOTOPE EFFECTS; KINETIC STEPS; RELATIVE TIMING; SOLVENT VISCOSITY; STEADY-STATE KINETICS; STOPPED FLOW; STOPPED-FLOW KINETICS; TIME-RESOLVED;

EID: 84874032081     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3016235     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins J. Biol. Chem. 269, 22459-22462
    • (1994) J. Biol. Chem. , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 2
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes Trends Biochem. Sci. 31, 276-283
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 3
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B. and Gutteridge, J. M. (1984) Oxygen toxicity, oxygen radicals, transition metals and disease Biochem. J. 219, 1-14
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 4
    • 34447638717 scopus 로고    scopus 로고
    • How do enzymes activate oxygen without inactivating themselves?
    • Klinman, J. P. (2007) How do enzymes activate oxygen without inactivating themselves? Acc. Chem. Res. 40, 325-333
    • (2007) Acc. Chem. Res. , vol.40 , pp. 325-333
    • Klinman, J.P.1
  • 5
  • 6
    • 1542664950 scopus 로고
    • One and two electron reduction of oxygen by 1,5-dihydroflavins
    • Eberlein, G. and Bruice, T. C. (1982) One and two electron reduction of oxygen by 1,5-dihydroflavins J. Am. Chem. Soc. 104, 1449-1452
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1449-1452
    • Eberlein, G.1    Bruice, T.C.2
  • 7
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla, S. and Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions Eur. J. Biochem. 181, 1-17
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 9
    • 78650858458 scopus 로고    scopus 로고
    • Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase
    • Pennati, A. and Gadda, G. (2011) Stabilization of an intermediate in the oxidative half-reaction of human liver glycolate oxidase Biochemistry 50, 1-3
    • (2011) Biochemistry , vol.50 , pp. 1-3
    • Pennati, A.1    Gadda, G.2
  • 10
    • 72049124811 scopus 로고    scopus 로고
    • Control of catalysis in flavin-dependent monooxygenases
    • Palfey, B. A. and McDonald, C. A. (2010) Control of catalysis in flavin-dependent monooxygenases Arch. Biochem. Biophys. 493, 26-36
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 26-36
    • Palfey, B.A.1    McDonald, C.A.2
  • 11
    • 0035909090 scopus 로고    scopus 로고
    • Mechanistic studies of cyclohexanone monooxygenase: Chemical properties of intermediates involved in catalysis
    • Sheng, D., Ballou, D. P., and Massey, V. (2001) Mechanistic studies of cyclohexanone monooxygenase: Chemical properties of intermediates involved in catalysis Biochemistry 40, 11156-11167
    • (2001) Biochemistry , vol.40 , pp. 11156-11167
    • Sheng, D.1    Ballou, D.P.2    Massey, V.3
  • 12
    • 79955750085 scopus 로고    scopus 로고
    • Hydrogen peroxide elimination from C4a-hydroperoxyflavin in a flavoprotein oxidase occurs through a single proton transfer from flavin N5 to a peroxide leaving group
    • Sucharitakul, J., Wongnate, T., and Chaiyen, P. (2011) Hydrogen peroxide elimination from C4a-hydroperoxyflavin in a flavoprotein oxidase occurs through a single proton transfer from flavin N5 to a peroxide leaving group J. Biol. Chem. 286, 16900-16909
    • (2011) J. Biol. Chem. , vol.286 , pp. 16900-16909
    • Sucharitakul, J.1    Wongnate, T.2    Chaiyen, P.3
  • 13
    • 80051480273 scopus 로고    scopus 로고
    • Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms
    • Thotsaporn, K., Chenprakhon, P., Sucharitakul, J., Mattevi, A., and Chaiyen, P. (2011) Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms J. Biol. Chem. 286, 28170-28180
    • (2011) J. Biol. Chem. , vol.286 , pp. 28170-28180
    • Thotsaporn, K.1    Chenprakhon, P.2    Sucharitakul, J.3    Mattevi, A.4    Chaiyen, P.5
  • 14
    • 0032537559 scopus 로고    scopus 로고
    • Oxygen reactivity of an NADH oxidase C42S mutant: Evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change
    • Mallett, T. C. and Claiborne, A. (1998) Oxygen reactivity of an NADH oxidase C42S mutant: Evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change Biochemistry 37, 8790-8802
    • (1998) Biochemistry , vol.37 , pp. 8790-8802
    • Mallett, T.C.1    Claiborne, A.2
  • 17
    • 84859376000 scopus 로고    scopus 로고
    • Oxygen activation in flavoprotein oxidases: The importance of being positive
    • Gadda, G. (2012) Oxygen activation in flavoprotein oxidases: The importance of being positive Biochemistry 51, 2662-2669
    • (2012) Biochemistry , vol.51 , pp. 2662-2669
    • Gadda, G.1
  • 18
    • 33745713811 scopus 로고    scopus 로고
    • On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase
    • Gadda, G., Fan, F., and Hoang, J. V. (2006) On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase Arch. Biochem. Biophys. 451, 182-187
    • (2006) Arch. Biochem. Biophys. , vol.451 , pp. 182-187
    • Gadda, G.1    Fan, F.2    Hoang, J.V.3
  • 19
    • 0348109494 scopus 로고    scopus 로고
    • Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: A bacterial enzyme involved in osmotic stress tolerance
    • Fan, F., Ghanem, M., and Gadda, G. (2004) Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: A bacterial enzyme involved in osmotic stress tolerance Arch. Biochem. Biophys. 421, 149-158
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 149-158
    • Fan, F.1    Ghanem, M.2    Gadda, G.3
  • 20
    • 0347594221 scopus 로고    scopus 로고
    • Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis
    • Ghanem, M., Fan, F., Francis, K., and Gadda, G. (2003) Spectroscopic and kinetic properties of recombinant choline oxidase from Arthrobacter globiformis Biochemistry 42, 15179-15188
    • (2003) Biochemistry , vol.42 , pp. 15179-15188
    • Ghanem, M.1    Fan, F.2    Francis, K.3    Gadda, G.4
  • 23
    • 29344449107 scopus 로고    scopus 로고
    • Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: Correlating reversible hydride transfer with environmentally enhanced tunneling
    • Fan, F. and Gadda, G. (2005) Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: Correlating reversible hydride transfer with environmentally enhanced tunneling J. Am. Chem. Soc. 127, 17954-17961
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17954-17961
    • Fan, F.1    Gadda, G.2
  • 24
    • 12344271332 scopus 로고    scopus 로고
    • On the catalytic mechanism of choline oxidase
    • Fan, F. and Gadda, G. (2005) On the catalytic mechanism of choline oxidase J. Am. Chem. Soc. 127, 2067-2074
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2067-2074
    • Fan, F.1    Gadda, G.2
  • 28
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., Jones, C., Henry, E., Hofrichter, J., and Eaton, W. (1992) The role of solvent viscosity in the dynamics of protein conformational changes Science 256, 1796-1798
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.2    Henry, E.3    Hofrichter, J.4    Eaton, W.5
  • 29
    • 0020348401 scopus 로고
    • Use of isotope effects to elucidate enzyme mechanisms
    • Cleland, W. W. (1982) Use of isotope effects to elucidate enzyme mechanisms CRC Crit. Rev. Biochem. 13, 385-428
    • (1982) CRC Crit. Rev. Biochem. , vol.13 , pp. 385-428
    • Cleland, W.W.1
  • 30
    • 0031053278 scopus 로고    scopus 로고
    • Determination of the Chemical Mechanism of Malic Enzyme by Isotope Effects
    • Edens, W. A., Urbauer, J. L., and Cleland, W. W. (1997) Determination of the Chemical Mechanism of Malic Enzyme by Isotope Effects Biochemistry 36, 1141-1147
    • (1997) Biochemistry , vol.36 , pp. 1141-1147
    • Edens, W.A.1    Urbauer, J.L.2    Cleland, W.W.3
  • 31
    • 78650947225 scopus 로고    scopus 로고
    • PH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
    • Ruangchan, N., Tongsook, C., Sucharitakul, J., and Chaiyen, P. (2011) pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase J. Biol. Chem. 286, 223-233
    • (2011) J. Biol. Chem. , vol.286 , pp. 223-233
    • Ruangchan, N.1    Tongsook, C.2    Sucharitakul, J.3    Chaiyen, P.4
  • 32
    • 84865428476 scopus 로고    scopus 로고
    • Role of Active Site Histidines in the Two Half-Reactions of the Aryl-Alcohol Oxidase Catalytic Cycle
    • Hernández-Ortega, A., Lucas, F., Ferreira, P., Medina, M., Guallar, V., and Martínez, A. T. (2012) Role of Active Site Histidines in the Two Half-Reactions of the Aryl-Alcohol Oxidase Catalytic Cycle Biochemistry 51, 6595-6608
    • (2012) Biochemistry , vol.51 , pp. 6595-6608
    • Hernández-Ortega, A.1    Lucas, F.2    Ferreira, P.3    Medina, M.4    Guallar, V.5    Martínez, A.T.6
  • 33
    • 83055179279 scopus 로고    scopus 로고
    • Insights on the Mechanism of Amine Oxidation Catalyzed by d -Arginine Dehydrogenase through pH and Kinetic Isotope Effects
    • Yuan, H., Xin, Y., Hamelberg, D., and Gadda, G. (2011) Insights on the Mechanism of Amine Oxidation Catalyzed by d -Arginine Dehydrogenase through pH and Kinetic Isotope Effects J. Am. Chem. Soc. 133, 18957-18965
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18957-18965
    • Yuan, H.1    Xin, Y.2    Hamelberg, D.3    Gadda, G.4
  • 34
    • 0000663213 scopus 로고
    • General Base Catalysis of Ester Hydrolysis
    • Jencks, W. P. and Carriuolo, J. (1961) General Base Catalysis of Ester Hydrolysis J. Am. Chem. Soc. 83, 1743-1750
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 1743-1750
    • Jencks, W.P.1    Carriuolo, J.2
  • 35
    • 50849101652 scopus 로고    scopus 로고
    • Identification of the oxygen activation site in monomeric sarcosine oxidase: Role of Lys265 in catalysis
    • Zhao, G., Bruckner, R. C., and Jorns, M. S. (2008) Identification of the oxygen activation site in monomeric sarcosine oxidase: Role of Lys265 in catalysis Biochemistry 47, 9124-9135
    • (2008) Biochemistry , vol.47 , pp. 9124-9135
    • Zhao, G.1    Bruckner, R.C.2    Jorns, M.S.3
  • 36
    • 79958065906 scopus 로고    scopus 로고
    • Pleiotropic impact of a single lysine mutation on biosynthesis of and catalysis by N-methyltryptophan oxidase
    • Bruckner, R. C., Winans, J., and Jorns, M. S. (2011) Pleiotropic impact of a single lysine mutation on biosynthesis of and catalysis by N-methyltryptophan oxidase Biochemistry 50, 4949-4962
    • (2011) Biochemistry , vol.50 , pp. 4949-4962
    • Bruckner, R.C.1    Winans, J.2    Jorns, M.S.3
  • 38
    • 0030739371 scopus 로고    scopus 로고
    • Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. Evidence for formation of a p-quinone methide intermediate
    • Fraaije, M. W. and van Berkel, W. J. (1997) Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. Evidence for formation of a p-quinone methide intermediate J. Biol. Chem. 272, 18111-18116
    • (1997) J. Biol. Chem. , vol.272 , pp. 18111-18116
    • Fraaije, M.W.1    Van Berkel, W.J.2
  • 39
    • 0027534454 scopus 로고
    • Substrate-specific enhancement of the oxidative half-reaction of monoamine oxidase
    • Tan, A. K. and Ramsay, R. R. (1993) Substrate-specific enhancement of the oxidative half-reaction of monoamine oxidase Biochemistry 32, 2137-2143
    • (1993) Biochemistry , vol.32 , pp. 2137-2143
    • Tan, A.K.1    Ramsay, R.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.