메뉴 건너뛰기




Volumn 51, Issue 13, 2012, Pages 2662-2669

Oxygen activation in flavoprotein oxidases: The importance of being positive

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINE OXIDATION; CATALYTIC MOTIF; CHOLINE OXIDASE; COFACTORS; DESOLVATION; ELECTROSTATIC STABILIZATION; N-METHYLTRYPTOPHAN OXIDASE; NON-POLAR; OXYGEN ACTIVATIONS; POSITIVE CHARGES; RATE ACCELERATION; RATE ENHANCEMENT; REACTION SITES; SARCOSINE OXIDASE; SECOND-ORDER RATE CONSTANTS; SEMIQUINONE RADICALS; SINGLE ELECTRON TRANSFER; TRANSITION STATE;

EID: 84859376000     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300227d     Document Type: Article
Times cited : (101)

References (75)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije, M. W. and Mattevi, A. (2000) Flavoenzymes: diverse catalysts with recurrent features Trends Biochem. Sci. 25, 126-132
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 5
    • 58849100936 scopus 로고    scopus 로고
    • Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases
    • Gadda, G. (2008) Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases Biochemistry 47, 13745-13753
    • (2008) Biochemistry , vol.47 , pp. 13745-13753
    • Gadda, G.1
  • 7
    • 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
  • 8
    • 78149342506 scopus 로고    scopus 로고
    • Steady-state kinetic mechanism and reductive half-reaction of d -arginine dehydrogenase from Pseudomonas aeruginosa
    • Yuan, H., Fu, G., Brooks, P. T., Weber, I., and Gadda, G. (2010) Steady-state kinetic mechanism and reductive half-reaction of d -arginine dehydrogenase from Pseudomonas aeruginosa Biochemistry 49, 9542-9550
    • (2010) Biochemistry , vol.49 , pp. 9542-9550
    • Yuan, H.1    Fu, G.2    Brooks, P.T.3    Weber, I.4    Gadda, G.5
  • 11
    • 0033614811 scopus 로고    scopus 로고
    • Nature of oxygen activation in glucose oxidase from Aspergillus niger: The importance of electrostatic stabilization in superoxide formation
    • Su, Q. and Klinman, J. P. (1999) Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation Biochemistry 38, 8572-8581
    • (1999) Biochemistry , vol.38 , pp. 8572-8581
    • Su, Q.1    Klinman, J.P.2
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 4444281751 scopus 로고    scopus 로고
    • The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase
    • Gadda, G., Powell, N. L., and Menon, P. (2004) The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase Arch. Biochem. Biophys. 430, 264-273
    • (2004) Arch. Biochem. Biophys. , vol.430 , pp. 264-273
    • Gadda, G.1    Powell, N.L.2    Menon, P.3
  • 17
    • 12344251747 scopus 로고    scopus 로고
    • On the catalytic role of the conserved active site residue His466 of choline oxidase
    • Ghanem, M. and Gadda, G. (2005) On the catalytic role of the conserved active site residue His466 of choline oxidase Biochemistry 44, 893-904
    • (2005) Biochemistry , vol.44 , pp. 893-904
    • Ghanem, M.1    Gadda, G.2
  • 18
    • 67650541861 scopus 로고    scopus 로고
    • Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase
    • Quaye, O., Cowins, S., and Gadda, G. (2009) Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase J. Biol. Chem. 284, 16990-16997
    • (2009) J. Biol. Chem. , vol.284 , pp. 16990-16997
    • Quaye, O.1    Cowins, S.2    Gadda, G.3
  • 19
    • 46049114878 scopus 로고    scopus 로고
    • On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase
    • Rungsrisuriyachai, K. and Gadda, G. (2008) On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase Biochemistry 47, 6762-6769
    • (2008) Biochemistry , vol.47 , pp. 6762-6769
    • Rungsrisuriyachai, K.1    Gadda, G.2
  • 20
    • 0004052075 scopus 로고
    • Oxford University Press, New York
    • Sawyer, D. T. (1991) Oxygen Chemistry, Oxford University Press, New York.
    • (1991) Oxygen Chemistry
    • Sawyer, D.T.1
  • 21
    • 0033570113 scopus 로고    scopus 로고
    • The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide. A reappraisal
    • Mayhew, S. G. (1999) The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide. A reappraisal Eur. J. Biochem. 265, 698-702
    • (1999) Eur. J. Biochem. , vol.265 , pp. 698-702
    • Mayhew, S.G.1
  • 22
    • 33745662190 scopus 로고    scopus 로고
    • Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life
    • Halliwell, B. (2006) Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life Plant Physiol. 141, 312-322
    • (2006) Plant Physiol. , vol.141 , pp. 312-322
    • Halliwell, B.1
  • 23
    • 0017784006 scopus 로고
    • 2 with dihydroflavins. 1. N-3,5-dimethyl-1,5-dihydrolumiflavin and 1,5-dihydroisoalloxazines
    • 2 with dihydroflavins. 1. N-3,5-dimethyl-1,5- dihydrolumiflavin and 1,5-dihydroisoalloxazines J. Am. Chem. Soc. 99, 7272-7286
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 7272-7286
    • Kemal, C.1    Chan, T.W.2    Bruice, R.C.3
  • 24
    • 84978937530 scopus 로고    scopus 로고
    • The reactivity of oxygen with flavoproteins
    • Massey, V. (2002) The reactivity of oxygen with flavoproteins Int. Congress Ser. 1233, 3-11
    • (2002) Int. Congress Ser. , vol.1233 , pp. 3-11
    • Massey, V.1
  • 26
  • 27
    • 70549103613 scopus 로고    scopus 로고
    • The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: Structural biology and biomolecular simulation
    • Baron, R., McCammon, J. A., and Mattevi, A. (2009) The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: structural biology and biomolecular simulation Curr. Opin. Struct. Biol. 19, 672-679
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 672-679
    • Baron, R.1    McCammon, J.A.2    Mattevi, A.3
  • 28
    • 43249129470 scopus 로고    scopus 로고
    • The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase
    • Chen, L., Lyubimov, A. Y., Brammer, L., Vrielink, A., and Sampson, N. S. (2008) The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase Biochemistry 47, 5368-5377
    • (2008) Biochemistry , vol.47 , pp. 5368-5377
    • Chen, L.1    Lyubimov, A.Y.2    Brammer, L.3    Vrielink, A.4    Sampson, N.S.5
  • 30
    • 77950407407 scopus 로고    scopus 로고
    • Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase
    • Finnegan, S., Agniswamy, J., Weber, I. T., and Gadda, G. (2010) Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase Biochemistry 49, 2952-2961
    • (2010) Biochemistry , vol.49 , pp. 2952-2961
    • Finnegan, S.1    Agniswamy, J.2    Weber, I.T.3    Gadda, G.4
  • 31
    • 0034840430 scopus 로고    scopus 로고
    • Life as aerobes: Are there simple rules for activation of dioxygen by enzymes?
    • Klinman, J. P. (2001) Life as aerobes: are there simple rules for activation of dioxygen by enzymes? J. Biol. Inorg. Chem. 6, 1-13
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 1-13
    • Klinman, J.P.1
  • 32
    • 79952094721 scopus 로고    scopus 로고
    • Importance of a serine proximal to the C(4a) and N(5) flavin atoms for hydride transfer in choline oxidase
    • Yuan, H. and Gadda, G. (2011) Importance of a serine proximal to the C(4a) and N(5) flavin atoms for hydride transfer in choline oxidase Biochemistry 50, 770-779
    • (2011) Biochemistry , vol.50 , pp. 770-779
    • Yuan, H.1    Gadda, G.2
  • 33
    • 77949505450 scopus 로고    scopus 로고
    • Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase
    • Rungsrisuriyachai, K. and Gadda, G. (2010) Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase Biochemistry 49, 2483-2490
    • (2010) Biochemistry , vol.49 , pp. 2483-2490
    • Rungsrisuriyachai, K.1    Gadda, G.2
  • 34
    • 77953727643 scopus 로고    scopus 로고
    • Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue
    • Quaye, O., Nguyen, T., Gannavaram, S., Pennati, A., and Gadda, G. (2010) Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue Arch. Biochem. Biophys. 499, 1-5
    • (2010) Arch. Biochem. Biophys. , vol.499 , pp. 1-5
    • Quaye, O.1    Nguyen, T.2    Gannavaram, S.3    Pennati, A.4    Gadda, G.5
  • 35
    • 77956177377 scopus 로고    scopus 로고
    • Structural and kinetic studies on the Ser101Ala variant of choline oxidase: Catalysis by compromise
    • Finnegan, S., Yuan, H., Wang, Y. F., Orville, A. M., Weber, I. T., and Gadda, G. (2010) Structural and kinetic studies on the Ser101Ala variant of choline oxidase: catalysis by compromise Arch. Biochem. Biophys. 501, 207-213
    • (2010) Arch. Biochem. Biophys. , vol.501 , pp. 207-213
    • Finnegan, S.1    Yuan, H.2    Wang, Y.F.3    Orville, A.M.4    Weber, I.T.5    Gadda, G.6
  • 36
    • 70350050563 scopus 로고    scopus 로고
    • The cluster of hydrophobic residues controls the entrance to the active site of choline oxidase
    • Xin, Y., Gadda, G., and Hamelberg, D. (2009) The cluster of hydrophobic residues controls the entrance to the active site of choline oxidase Biochemistry 48, 9599-9605
    • (2009) Biochemistry , vol.48 , pp. 9599-9605
    • Xin, Y.1    Gadda, G.2    Hamelberg, D.3
  • 37
    • 69849104100 scopus 로고    scopus 로고
    • Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase
    • Quaye, O. and Gadda, G. (2009) Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase Arch. Biochem. Biophys. 489, 10-14
    • (2009) Arch. Biochem. Biophys. , vol.489 , pp. 10-14
    • Quaye, O.1    Gadda, G.2
  • 38
    • 60749096264 scopus 로고    scopus 로고
    • Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase
    • Orville, A. M., Lountos, G. T., Finnegan, S., Gadda, G., and Prabhakar, R. (2009) Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase Biochemistry 48, 720-728
    • (2009) Biochemistry , vol.48 , pp. 720-728
    • Orville, A.M.1    Lountos, G.T.2    Finnegan, S.3    Gadda, G.4    Prabhakar, R.5
  • 39
    • 37849031214 scopus 로고    scopus 로고
    • Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase
    • Quaye, O., Lountos, G. T., Fan, F., Orville, A. M., and Gadda, G. (2008) Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase Biochemistry 47, 243-256
    • (2008) Biochemistry , vol.47 , pp. 243-256
    • Quaye, O.1    Lountos, G.T.2    Fan, F.3    Orville, A.M.4    Gadda, G.5
  • 40
    • 58849110962 scopus 로고    scopus 로고
    • Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase
    • Finnegan, S. and Gadda, G. (2008) Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase Biochemistry 47, 13850-13861
    • (2008) Biochemistry , vol.47 , pp. 13850-13861
    • Finnegan, S.1    Gadda, G.2
  • 41
    • 0042622631 scopus 로고    scopus 로고
    • Kinetic mechanism of choline oxidase from Arthrobacter globiformis
    • Gadda, G. (2003) Kinetic mechanism of choline oxidase from Arthrobacter globiformis Biochim. Biophys. Acta 1646, 112-118
    • (2003) Biochim. Biophys. Acta , vol.1646 , pp. 112-118
    • Gadda, G.1
  • 42
    • 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
  • 43
    • 33644868234 scopus 로고    scopus 로고
    • Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase
    • Ghanem, M. and Gadda, G. (2006) Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase Biochemistry 45, 3437-3447
    • (2006) Biochemistry , vol.45 , pp. 3437-3447
    • Ghanem, M.1    Gadda, G.2
  • 44
    • 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
  • 45
    • 32444447830 scopus 로고    scopus 로고
    • Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde
    • Fan, F., Germann, M. W., and Gadda, G. (2006) Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde Biochemistry 45, 1979-1986
    • (2006) Biochemistry , vol.45 , pp. 1979-1986
    • Fan, F.1    Germann, M.W.2    Gadda, G.3
  • 46
    • 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
  • 47
    • 0026544690 scopus 로고
    • GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities
    • Cavener, D. R. (1992) GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities J. Mol. Biol. 223, 811-814
    • (1992) J. Mol. Biol. , vol.223 , pp. 811-814
    • Cavener, D.R.1
  • 48
    • 67650480250 scopus 로고    scopus 로고
    • Whats in a covalent bond? on the role and formation of covalently bound flavin cofactors
    • Heuts, D. P., Scrutton, N. S., McIntire, W. S., and Fraaije, M. W. (2009) Whats in a covalent bond? On the role and formation of covalently bound flavin cofactors FEBS J. 276, 3405-3427
    • (2009) FEBS J. , vol.276 , pp. 3405-3427
    • Heuts, D.P.1    Scrutton, N.S.2    McIntire, W.S.3    Fraaije, M.W.4
  • 49
    • 34249676309 scopus 로고    scopus 로고
    • An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase
    • Fan, F. and Gadda, G. (2007) An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase Biochemistry 46, 6402-6408
    • (2007) Biochemistry , vol.46 , pp. 6402-6408
    • Fan, F.1    Gadda, G.2
  • 51
    • 77957269392 scopus 로고    scopus 로고
    • Conformational changes and substrate recognition in Pseudomonas aeruginosa d -arginine dehydrogenase
    • Fu, G., Yuan, H., Li, C., Lu, C. D., Gadda, G., and Weber, I. T. (2010) Conformational changes and substrate recognition in Pseudomonas aeruginosa d -arginine dehydrogenase Biochemistry 49, 8535-8545
    • (2010) Biochemistry , vol.49 , pp. 8535-8545
    • Fu, G.1    Yuan, H.2    Li, C.3    Lu, C.D.4    Gadda, G.5    Weber, I.T.6
  • 52
    • 0029155316 scopus 로고
    • 2 mutant crystallized in the presence of lactate or phenyl lactate
    • 2 mutant crystallized in the presence of lactate or phenyl lactate Biochemistry 34, 9840-9850
    • (1995) Biochemistry , vol.34 , pp. 9840-9850
    • Tegoni, M.1    Begotti, S.2    Cambillau, C.3
  • 53
    • 39749159159 scopus 로고    scopus 로고
    • Active site and loop 4 movements within human glycolate oxidase: Implications for substrate specificity and drug design
    • Murray, M. S., Holmes, R. P., and Lowther, W. T. (2008) Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design Biochemistry 47, 2439-2449
    • (2008) Biochemistry , vol.47 , pp. 2439-2449
    • Murray, M.S.1    Holmes, R.P.2    Lowther, W.T.3
  • 54
    • 0030940522 scopus 로고    scopus 로고
    • Three-dimensional structures of glycolate oxidase with bound active-site inhibitors
    • Stenberg, K. and Lindqvist, Y. (1997) Three-dimensional structures of glycolate oxidase with bound active-site inhibitors Protein Sci. 6, 1009-1015
    • (1997) Protein Sci. , vol.6 , pp. 1009-1015
    • Stenberg, K.1    Lindqvist, Y.2
  • 55
    • 72049099611 scopus 로고    scopus 로고
    • Oxidation of amines by flavoproteins
    • Fitzpatrick, P. F. (2010) Oxidation of amines by flavoproteins Arch. Biochem. Biophys. 493, 13-25
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 13-25
    • Fitzpatrick, P.F.1
  • 56
    • 1942485882 scopus 로고    scopus 로고
    • Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations
    • Fitzpatrick, P. F. (2004) Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations Bioorg. Chem. 32, 125-139
    • (2004) Bioorg. Chem. , vol.32 , pp. 125-139
    • Fitzpatrick, P.F.1
  • 57
    • 0017394294 scopus 로고
    • Mechanistic features of the d -amino acid oxidase reaction studied by double stopped flow spectrophotometry
    • Porter, D. J., Voet, J. G., and Bright, H. J. (1977) Mechanistic features of the d -amino acid oxidase reaction studied by double stopped flow spectrophotometry J. Biol. Chem. 252, 4464-4473
    • (1977) J. Biol. Chem. , vol.252 , pp. 4464-4473
    • Porter, D.J.1    Voet, J.G.2    Bright, H.J.3
  • 58
    • 0033551820 scopus 로고    scopus 로고
    • Influence of flavin analogue structure on the catalytic activities and flavinylation reactions of recombinant human liver monoamine oxidases A and B
    • Miller, J. R. and Edmondson, D. E. (1999) Influence of flavin analogue structure on the catalytic activities and flavinylation reactions of recombinant human liver monoamine oxidases A and B J. Biol. Chem. 274, 23515-23525
    • (1999) J. Biol. Chem. , vol.274 , pp. 23515-23525
    • Miller, J.R.1    Edmondson, D.E.2
  • 59
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    • Binda, C., Li, M., Hubalek, F., Restelli, N., Edmondson, D. E., and Mattevi, A. (2003) Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures Proc. Natl. Acad. Sci. U.S.A 100, 9750-9755
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, N.4    Edmondson, D.E.5    Mattevi, A.6
  • 60
    • 77953538248 scopus 로고    scopus 로고
    • A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase
    • Henderson Pozzi, M. and Fitzpatrick, P. F. (2010) A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase Arch. Biochem. Biophys. 498, 83-88
    • (2010) Arch. Biochem. Biophys. , vol.498 , pp. 83-88
    • Henderson Pozzi, M.1    Fitzpatrick, P.F.2
  • 61
    • 78650123938 scopus 로고    scopus 로고
    • Mechanistic studies of the yeast polyamine oxidase Fms1: Kinetic mechanism, substrate specificity, and pH dependence
    • Adachi, M. S., Torres, J. M., and Fitzpatrick, P. F. (2010) Mechanistic studies of the yeast polyamine oxidase Fms1: kinetic mechanism, substrate specificity, and pH dependence Biochemistry 49, 10440-10448
    • (2010) Biochemistry , vol.49 , pp. 10440-10448
    • Adachi, M.S.1    Torres, J.M.2    Fitzpatrick, P.F.3
  • 62
    • 0038419788 scopus 로고    scopus 로고
    • Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase
    • Wu, T., Yankovskaya, V., and McIntire, W. S. (2003) Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase J. Biol. Chem. 278, 20514-20525
    • (2003) J. Biol. Chem. , vol.278 , pp. 20514-20525
    • Wu, T.1    Yankovskaya, V.2    McIntire, W.S.3
  • 63
    • 0141706648 scopus 로고    scopus 로고
    • Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
    • Knapp, M. J. and Klinman, J. P. (2003) Kinetic studies of oxygen reactivity in soybean lipoxygenase-1 Biochemistry 42, 11466-11475
    • (2003) Biochemistry , vol.42 , pp. 11466-11475
    • Knapp, M.J.1    Klinman, J.P.2
  • 64
    • 0032490094 scopus 로고    scopus 로고
    • Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation
    • Francisco, W. A., Tian, G., Fitzpatrick, P. F., and Klinman, J. P. (1998) Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: evidence of rate limiting oxygen activation J. Am. Chem. Soc. 120, 4057-4062
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4057-4062
    • Francisco, W.A.1    Tian, G.2    Fitzpatrick, P.F.3    Klinman, J.P.4
  • 65
    • 0037137223 scopus 로고    scopus 로고
    • Binding of dioxygen to non-metal sites in proteins: Exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha
    • Goto, Y. and Klinman, J. P. (2002) Binding of dioxygen to non-metal sites in proteins: exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha Biochemistry 41, 13637-13643
    • (2002) Biochemistry , vol.41 , pp. 13637-13643
    • Goto, Y.1    Klinman, J.P.2
  • 66
    • 49749144875 scopus 로고    scopus 로고
    • Detection of a C4a-hydroperoxyflavin intermediate in the reaction of a flavoprotein oxidase
    • Sucharitakul, J., Prongjit, M., Haltrich, D., and Chaiyen, P. (2008) Detection of a C4a-hydroperoxyflavin intermediate in the reaction of a flavoprotein oxidase Biochemistry 47, 8485-8490
    • (2008) Biochemistry , vol.47 , pp. 8485-8490
    • Sucharitakul, J.1    Prongjit, M.2    Haltrich, D.3    Chaiyen, P.4
  • 67
    • 50549155520 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection Biochim. Biophys. Acta 67, 188-196
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 188-196
    • Cleland, W.W.1
  • 68
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations Biochim. Biophys. Acta 67, 104-137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 71
    • 59849110412 scopus 로고    scopus 로고
    • A pH switch affects the steady-state kinetic mechanism of pyranose 2-oxidase from Trametes ochracea
    • Rungsrisuriyachai, K. and Gadda, G. (2009) A pH switch affects the steady-state kinetic mechanism of pyranose 2-oxidase from Trametes ochracea Arch. Biochem. Biophys. 483, 10-15
    • (2009) Arch. Biochem. Biophys. , vol.483 , pp. 10-15
    • Rungsrisuriyachai, K.1    Gadda, G.2
  • 72
    • 71449113304 scopus 로고    scopus 로고
    • Involvement of ionizable groups in catalysis of human liver glycolate oxidase
    • Pennati, A. and Gadda, G. (2009) Involvement of ionizable groups in catalysis of human liver glycolate oxidase J. Biol. Chem. 284, 31214-31222
    • (2009) J. Biol. Chem. , vol.284 , pp. 31214-31222
    • Pennati, A.1    Gadda, G.2
  • 73
    • 0034673122 scopus 로고    scopus 로고
    • Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole
    • Gadda, G. and Fitzpatrick, P. F. (2000) Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole Biochemistry 39, 1400-1405
    • (2000) Biochemistry , vol.39 , pp. 1400-1405
    • Gadda, G.1    Fitzpatrick, P.F.2
  • 74
    • 0018690805 scopus 로고
    • Plotting methods for analyzing enzyme rate data
    • Rudolph, F. B. and Fromm, H. J. (1979) Plotting methods for analyzing enzyme rate data Methods Enzymol. 63, 138-159
    • (1979) Methods Enzymol. , vol.63 , pp. 138-159
    • Rudolph, F.B.1    Fromm, H.J.2
  • 75
    • 77953662325 scopus 로고    scopus 로고
    • Identification of a hypothetical protein from Podospora anserina as a nitroalkane oxidase
    • Tormos, J. R., Taylor, A. B., Daubner, S. C., Hart, P. J., and Fitzpatrick, P. F. (2010) Identification of a hypothetical protein from Podospora anserina as a nitroalkane oxidase Biochemistry 49, 5035-5041
    • (2010) Biochemistry , vol.49 , pp. 5035-5041
    • Tormos, J.R.1    Taylor, A.B.2    Daubner, S.C.3    Hart, P.J.4    Fitzpatrick, P.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.