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Volumn 275, Issue 13, 2008, Pages 3278-3289

Mammalian xanthine oxidoreductase - Mechanism of transition from xanthine dehydrogenase to xanthine oxidase

Author keywords

cation interaction; Flavin semiquinone; Hydrogen peroxide; Iron sulfur center; Molybdopterin cofactor; Reactive oxygen species; Superoxide; Xanthine dehydrogenase; Xanthine oxidase; Xanthine oxidoreductase

Indexed keywords

CYSTEINE; HYDROGEN PEROXIDE; MOLYBDENUM; SUPEROXIDE; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE;

EID: 44949262935     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06489.x     Document Type: Review
Times cited : (303)

References (79)
  • 1
    • 0000417337 scopus 로고
    • Molybdenum iron-sulfur flavin hydroxylases and related enzymes
    • In. Boyer, P.D., ed. pp. Academic Press, New York, NY.
    • Bray RC (1975) Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In The Enzymes XII (Boyer PD, ed. pp. 300 419. Academic Press, New York, NY.
    • (1975) The Enzymes XII , pp. 300-419
    • Bray, R.C.1
  • 3
    • 0024554561 scopus 로고
    • The purine path to chemotherapy
    • Elion GB (1989) The purine path to chemotherapy. Science 244, 41 47.
    • (1989) Science , vol.244 , pp. 41-47
    • Elion, G.B.1
  • 4
    • 51249194871 scopus 로고
    • Über das Verhalten der Kuhmilch gegen Methyleneblau und seine Verwendung zur Unterscheidung von ungekochter und gekochter Milch
    • Schardinger F (1902) Über das Verhalten der Kuhmilch gegen Methyleneblau und seine Verwendung zur Unterscheidung von ungekochter und gekochter Milch. Z Untersuch Nahrungs Genussmittel 5, 1113 1121.
    • (1902) Z Untersuch Nahrungs Genussmittel , vol.5 , pp. 1113-1121
    • Schardinger, F.1
  • 5
    • 0009672484 scopus 로고
    • Studies on xanthine oxidase: The specificity of the system
    • Dixon M (1926) Studies on xanthine oxidase: the specificity of the system. Biochem J 20, 703 718.
    • (1926) Biochem J , vol.20 , pp. 703-718
    • Dixon, M.1
  • 6
    • 18844406618 scopus 로고
    • Note on the vitamin content of milk
    • Hopkins FG (1920) Note on the vitamin content of milk. Biochem J 14, 721 724.
    • (1920) Biochem J , vol.14 , pp. 721-724
    • Hopkins, F.G.1
  • 7
    • 0001996816 scopus 로고
    • Xanthine oxidase: Purification and properties
    • Ball EG (1939) Xanthine oxidase: purification and properties. J Biol Chem 128, 51 67.
    • (1939) J Biol Chem , vol.128 , pp. 51-67
    • Ball, E.G.1
  • 8
    • 0014217059 scopus 로고
    • Purification and properties of chicken liver xanthine dehydrogenase
    • Rajagopalan KV Handler P (1967) Purification and properties of chicken liver xanthine dehydrogenase. J Biol Chem 242, 4097 4107.
    • (1967) J Biol Chem , vol.242 , pp. 4097-4107
    • Rajagopalan, K.V.1    Handler, P.2
  • 9
    • 0016539882 scopus 로고
    • Xanthine dehydrogenase accumulation in developing Drosophila eyes
    • Barrett D Davidson NA (1975) Xanthine dehydrogenase accumulation in developing Drosophila eyes. J Insect Physiol 21, 1447 1452.
    • (1975) J Insect Physiol , vol.21 , pp. 1447-1452
    • Barrett, D.1    Davidson, N.A.2
  • 10
    • 0014294662 scopus 로고
    • Regulation of xanthine oxidase in rat liver: Modifications of the enzyme activity of rat liver supernatant on storage at 20 degrees
    • Della Corte E Stirpe F (1968) Regulation of xanthine oxidase in rat liver: modifications of the enzyme activity of rat liver supernatant on storage at 20 degrees. Biochem J 108, 349 351.
    • (1968) Biochem J , vol.108 , pp. 349-351
    • Della Corte, E.1    Stirpe, F.2
  • 11
    • 0014690734 scopus 로고
    • The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O)
    • Stirpe F Della Corte E (1969) The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O). J Biol Chem 244, 3855 3863.
    • (1969) J Biol Chem , vol.244 , pp. 3855-3863
    • Stirpe, F.1    Della Corte, E.2
  • 12
    • 0015298096 scopus 로고
    • The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme
    • Della Corte E Stirpe F (1972) The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem J 126, 739 745.
    • (1972) Biochem J , vol.126 , pp. 739-745
    • Della Corte, E.1    Stirpe, F.2
  • 13
    • 0015299250 scopus 로고
    • Xanthine oxidase type D (dehydrogenase) in the intestine and other organs of the rat
    • Battelli MG, Della Corte E Stirpe F (1972) Xanthine oxidase type D (dehydrogenase) in the intestine and other organs of the rat. Biochem J 126, 747 749.
    • (1972) Biochem J , vol.126 , pp. 747-749
    • Battelli, M.G.1    Della Corte, E.2    Stirpe, F.3
  • 14
    • 0020198381 scopus 로고
    • Preparation of bovine milk xanthine oxidase as a dehydrogenase form
    • Nakamura M Yamazaki I (1982) Preparation of bovine milk xanthine oxidase as a dehydrogenase form. J Biochem (Tokyo) 92, 1279 1286.
    • (1982) J Biochem (Tokyo) , vol.92 , pp. 1279-1286
    • Nakamura, M.1    Yamazaki, I.2
  • 15
    • 0017286148 scopus 로고
    • 2-dependent (type O) forms of rat liver xanthine dehydrogenase
    • 2-dependent (type O) forms of rat liver xanthine dehydrogenase. Arch Biochem Biophys 172, 354 364.
    • (1976) Arch Biochem Biophys , vol.172 , pp. 354-364
    • Waud, W.R.1    Rajagopalan, K.V.2
  • 16
    • 0024360669 scopus 로고
    • 2-dependent types of rat liver xanthine dehydrogenase
    • 2-dependent types of rat liver xanthine dehydrogenase. J Biol Chem 264, 10015 10022.
    • (1989) J Biol Chem , vol.264 , pp. 10015-10022
    • Saito, T.1    Nishino, T.2
  • 17
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244, 6049 6055.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 18
    • 0014446671 scopus 로고
    • Electron-spin-resonance evidence for enzymic reduction of oxygen to a free radical, the superoxide ion
    • Knowles PF, Gibson JF, Pick FM Bray RC (1969) Electron-spin-resonance evidence for enzymic reduction of oxygen to a free radical, the superoxide ion. Biochem J 111, 53 58.
    • (1969) Biochem J , vol.111 , pp. 53-58
    • Knowles, P.F.1    Gibson, J.F.2    Pick, F.M.3    Bray, R.C.4
  • 19
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord JM (1985) Oxygen-derived free radicals in postischemic tissue injury. N Engl J Med 312, 159 163.
    • (1985) N Engl J Med , vol.312 , pp. 159-163
    • McCord, J.M.1
  • 20
    • 0037105296 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase: Where are we now
    • Harrison R (2002) Structure and function of xanthine oxidoreductase: where are we now Free Radic Biol Med 33, 774 797.
    • (2002) Free Radic Biol Med , vol.33 , pp. 774-797
    • Harrison, R.1
  • 21
    • 1642484244 scopus 로고    scopus 로고
    • Xanthine oxidoreductase and cardiovascular disease: Molecular mechanisms and pathophysiological implications
    • Berry CE Hare JM (2004) Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. J Physiol 555, 589 606.
    • (2004) J Physiol , vol.555 , pp. 589-606
    • Berry, C.E.1    Hare, J.M.2
  • 22
    • 0037115712 scopus 로고    scopus 로고
    • The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: Gene sharing in the lactating mammary gland
    • Vorbach C, Scriven A Capecchi MR (2002) The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary gland. Genes Dev 16, 3223 3235.
    • (2002) Genes Dev , vol.16 , pp. 3223-3235
    • Vorbach, C.1    Scriven, A.2    Capecchi, M.R.3
  • 24
    • 0029347181 scopus 로고
    • Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenase
    • Hille R Nishino T (1995) Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenase. FASEB J 9, 995 1003.
    • (1995) FASEB J , vol.9 , pp. 995-1003
    • Hille, R.1    Nishino, T.2
  • 25
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96, 2757 2816.
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 26
    • 33646900495 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase
    • Hille R (2006) Structure and function of xanthine oxidoreductase. Eur J Inorg Chem 2006, 1913 1926.
    • (2006) Eur J Inorg Chem , vol.2006 , pp. 1913-1926
    • Hille, R.1
  • 27
    • 36949002370 scopus 로고    scopus 로고
    • Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: Roles of active site residues in binding and activation of purine substrate
    • Yamaguchi Y, Matsumura T, Ichida K, Okamoto K Nishino T (2007) Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate. J Biochem (Tokyo) 141, 513 524.
    • (2007) J Biochem (Tokyo) , vol.141 , pp. 513-524
    • Yamaguchi, Y.1    Matsumura, T.2    Ichida, K.3    Okamoto, K.4    Nishino, T.5
  • 28
    • 38449123646 scopus 로고    scopus 로고
    • Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase
    • Asai R, Nishino T, Matsumura T, Okamoto K, Igarashi K, Pai EF Nishino T (2007) Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase. J Biochem (Tokyo) 141, 525 534.
    • (2007) J Biochem (Tokyo) , vol.141 , pp. 525-534
    • Asai, R.1    Nishino, T.2    Matsumura, T.3    Okamoto, K.4    Igarashi, K.5    Pai, E.F.6    Nishino, T.7
  • 29
    • 21644469594 scopus 로고    scopus 로고
    • Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: Identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant
    • Nishino T, Okamoto K, Kawaguchi Y, Hori H, Matsumura T, Eger BT, Pai EF Nishino T (2005) Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant. J Biol Chem 280, 24888 24894.
    • (2005) J Biol Chem , vol.280 , pp. 24888-24894
    • Nishino, T.1    Okamoto, K.2    Kawaguchi, Y.3    Hori, H.4    Matsumura, T.5    Eger, B.T.6    Pai, E.F.7    Nishino, T.8
  • 30
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
    • Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T Pai EF (2000) Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc Natl Acad Sci USA 97, 10723 10728.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Nishino, T.5    Pai, E.F.6
  • 32
    • 0030824355 scopus 로고    scopus 로고
    • Milk xanthine oxidoreductase: The first one hundred years
    • Massey V Harris CM (1997) Milk xanthine oxidoreductase: the first one hundred years. Biochem Soc Trans 25, 750 755.
    • (1997) Biochem Soc Trans , vol.25 , pp. 750-755
    • Massey, V.1    Harris, C.M.2
  • 33
    • 0033582419 scopus 로고    scopus 로고
    • Role of the flavin midpoint potential and NAD binding in determining NAD versus oxygen reactivity of xanthine oxidoreductase
    • Harris CM, Sanders SA Massey V (1999) Role of the flavin midpoint potential and NAD binding in determining NAD versus oxygen reactivity of xanthine oxidoreductase. J Biol Chem 274, 4561 4569.
    • (1999) J Biol Chem , vol.274 , pp. 4561-4569
    • Harris, C.M.1    Sanders, S.A.2    Massey, V.3
  • 34
    • 0030928460 scopus 로고    scopus 로고
    • The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radical
    • Harris CM Massey V (1997) The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radical. J Biol Chem 272, 8370 8379.
    • (1997) J Biol Chem , vol.272 , pp. 8370-8379
    • Harris, C.M.1    Massey, V.2
  • 35
    • 0028069815 scopus 로고
    • The conversion of xanthine dehydrogenase to xanthine oxidase and the role of the enzyme in reperfusion injury
    • Nishino T (1994) The conversion of xanthine dehydrogenase to xanthine oxidase and the role of the enzyme in reperfusion injury. J Biochem (Tokyo) 116, 1 6.
    • (1994) J Biochem (Tokyo) , vol.116 , pp. 1-6
    • Nishino, T.1
  • 36
    • 0025143109 scopus 로고
    • 2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin
    • 2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin. J Biol Chem 265, 14170 14175.
    • (1990) J Biol Chem , vol.265 , pp. 14170-14175
    • Amaya, Y.1    Yamazaki, K.2    Sato, M.3    Noda, K.4    Nishino, T.5    Nishino, T.6
  • 37
    • 0027420799 scopus 로고
    • Electron transfer process in milk xanthine dehydrogenase as studied by pulse radiolysis
    • Kobayashi K, Miki M, Okamoto K Nishino T (1993) Electron transfer process in milk xanthine dehydrogenase as studied by pulse radiolysis. J Biol Chem 268, 24642 24646.
    • (1993) J Biol Chem , vol.268 , pp. 24642-24646
    • Kobayashi, K.1    Miki, M.2    Okamoto, K.3    Nishino, T.4
  • 38
    • 0014669756 scopus 로고
    • The preparation and properties of deflavo xanthine oxidase
    • Komai H, Massey V Palmer G (1969) The preparation and properties of deflavo xanthine oxidase. J Biol Chem 244, 1692 1700.
    • (1969) J Biol Chem , vol.244 , pp. 1692-1700
    • Komai, H.1    Massey, V.2    Palmer, G.3
  • 39
    • 0015500324 scopus 로고
    • Studies on the dissociation of flavin adenine dinucleotide from metalloflavoproteins
    • Kanda M, Brady FO, Rajagopalan KV Handler P (1972) Studies on the dissociation of flavin adenine dinucleotide from metalloflavoproteins. J Biol Chem 247, 765 770.
    • (1972) J Biol Chem , vol.247 , pp. 765-770
    • Kanda, M.1    Brady, F.O.2    Rajagopalan, K.V.3    Handler, P.4
  • 40
    • 0031940235 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes
    • Leimkuhler S, Kern M, Solomon PS, McEwan AG, Schwarz G, Mendel RR Klipp W (1998) Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes. Mol Microbiol 27, 853 869.
    • (1998) Mol Microbiol , vol.27 , pp. 853-869
    • Leimkuhler, S.1    Kern, M.2    Solomon, P.S.3    McEwan, A.G.4    Schwarz, G.5    Mendel, R.R.6    Klipp, W.7
  • 41
    • 0036153761 scopus 로고    scopus 로고
    • Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus
    • Truglio JJ, Theis K, Leimkuhler S, Rappa R, Rajagopalan KV Kisker C (2002) Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10, 115 125.
    • (2002) Structure , vol.10 , pp. 115-125
    • Truglio, J.J.1    Theis, K.2    Leimkuhler, S.3    Rappa, R.4    Rajagopalan, K.V.5    Kisker, C.6
  • 42
    • 1942534565 scopus 로고    scopus 로고
    • Cooperative catalysis in the homodimer subunits of xanthine oxidase
    • Tai LA Hwang KC (2004) Cooperative catalysis in the homodimer subunits of xanthine oxidase. Biochemistry 43, 4869 4876.
    • (2004) Biochemistry , vol.43 , pp. 4869-4876
    • Tai, L.A.1    Hwang, K.C.2
  • 45
    • 34250364587 scopus 로고    scopus 로고
    • The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatus
    • Pauff JM, Hemann CF, Junemann N, Leimkuhler S Hille R (2007) The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatus. J Biol Chem 282, 12785 12790.
    • (2007) J Biol Chem , vol.282 , pp. 12785-12790
    • Pauff, J.M.1    Hemann, C.F.2    Junemann, N.3    Leimkuhler, S.4    Hille, R.5
  • 46
    • 17244368599 scopus 로고    scopus 로고
    • Freeze-quench magnetic circular dichroism spectroscopic study of the 'very rapid' intermediate in xanthine oxidase
    • Jones RM, Inscore FE, Hille R Kirk ML (1999) Freeze-quench magnetic circular dichroism spectroscopic study of the 'very rapid' intermediate in xanthine oxidase. Inorg Chem 38, 4963 4970.
    • (1999) Inorg Chem , vol.38 , pp. 4963-4970
    • Jones, R.M.1    Inscore, F.E.2    Hille, R.3    Kirk, M.L.4
  • 47
    • 2542612969 scopus 로고    scopus 로고
    • The crystal structure of xanthine oxidoreductase during catalysis: Implications for reaction mechanism and enzyme inhibition
    • Okamoto K, Matsumoto K, Hille R, Eger BT, Pai EF Nishino T (2004) The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition. Proc Natl Acad Sci USA 101, 7931 7936.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7931-7936
    • Okamoto, K.1    Matsumoto, K.2    Hille, R.3    Eger, B.T.4    Pai, E.F.5    Nishino, T.6
  • 49
    • 4644366935 scopus 로고    scopus 로고
    • The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase
    • Leimkuhler S, Stockert AL, Igarashi K, Nishino T Hille R (2004) The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. J Biol Chem 279, 40437 40444.
    • (2004) J Biol Chem , vol.279 , pp. 40437-40444
    • Leimkuhler, S.1    Stockert, A.L.2    Igarashi, K.3    Nishino, T.4    Hille, R.5
  • 50
    • 34447135008 scopus 로고    scopus 로고
    • Oxidation reaction by xanthine oxidase: Theoretical study of reaction mechanism
    • Amano T, Ochi N, Sato H Sakaki S (2007) Oxidation reaction by xanthine oxidase: theoretical study of reaction mechanism. J Am Chem Soc 129, 8131 8138.
    • (2007) J Am Chem Soc , vol.129 , pp. 8131-8138
    • Amano, T.1    Ochi, N.2    Sato, H.3    Sakaki, S.4
  • 51
    • 0037449776 scopus 로고    scopus 로고
    • An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition
    • Okamoto K, Eger BT, Nishino T, Kondo S, Pai EF Nishino T (2003) An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition. J Biol Chem 278, 1848 1855.
    • (2003) J Biol Chem , vol.278 , pp. 1848-1855
    • Okamoto, K.1    Eger, B.T.2    Nishino, T.3    Kondo, S.4    Pai, E.F.5    Nishino, T.6
  • 52
    • 6344278025 scopus 로고    scopus 로고
    • Y-700 [1-[3-Cyano-4-(2,2-dimethylpropoxy)phenyl]-1H-pyrazole-4-carboxylic acid]: A potent xanthine oxidoreductase inhibitor with hepatic excretion
    • Fukunari A, Okamoto K, Nishino T, Eger BT, Pai EF, Kamezawa M, Yamada I Kato N (2004) Y-700 [1-[3-Cyano-4-(2,2-dimethylpropoxy)phenyl]-1H-pyrazole-4- carboxylic acid]: a potent xanthine oxidoreductase inhibitor with hepatic excretion. J Pharmacol Exp Ther 311, 519 528.
    • (2004) J Pharmacol Exp Ther , vol.311 , pp. 519-528
    • Fukunari, A.1    Okamoto, K.2    Nishino, T.3    Eger, B.T.4    Pai, E.F.5    Kamezawa, M.6    Yamada, I.7    Kato, N.8
  • 53
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • Garattini E, Mendel R, Romao MJ, Wright R Terao M (2003) Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372, 15 32.
    • (2003) Biochem J , vol.372 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 54
    • 0023693849 scopus 로고
    • Rapid reaction studies on the reduction and oxidation of chicken liver xanthine dehydrogenase by the xanthine/urate and NAD/NADH couples
    • Schopfer LM, Massey V Nishino T (1988) Rapid reaction studies on the reduction and oxidation of chicken liver xanthine dehydrogenase by the xanthine/urate and NAD/NADH couples. J Biol Chem 263, 13528 13538.
    • (1988) J Biol Chem , vol.263 , pp. 13528-13538
    • Schopfer, L.M.1    Massey, V.2    Nishino, T.3
  • 55
    • 41949116623 scopus 로고    scopus 로고
    • Substrate orientation in xanthine oxidase: Crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurine
    • Pauff JM, Zhang J, Bell CE Hille R (2008) Substrate orientation in xanthine oxidase: crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurine. J Biol Chem 283, 4818 4824.
    • (2008) J Biol Chem , vol.283 , pp. 4818-4824
    • Pauff, J.M.1    Zhang, J.2    Bell, C.E.3    Hille, R.4
  • 56
    • 0026322388 scopus 로고
    • The reductive half-reaction of xanthine oxidase. Identification of spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine
    • McWhirter RB Hille R (1991) The reductive half-reaction of xanthine oxidase. Identification of spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine. J Biol Chem 266, 23724 23731.
    • (1991) J Biol Chem , vol.266 , pp. 23724-23731
    • McWhirter, R.B.1    Hille, R.2
  • 57
    • 0014669771 scopus 로고
    • Studies on milk xanthine oxidase. Some spectral and kinetic properties
    • Massey V, Brumby PE Komai H (1969) Studies on milk xanthine oxidase. Some spectral and kinetic properties. J Biol Chem 244, 1682 1691.
    • (1969) J Biol Chem , vol.244 , pp. 1682-1691
    • Massey, V.1    Brumby, P.E.2    Komai, H.3
  • 58
    • 0034029284 scopus 로고    scopus 로고
    • Sequence motif-specific assignment of two [2Fe-2S] clusters in rat xanthine oxidoreductase studied by site-directed mutagenesis
    • Iwasaki T, Okamoto K, Nishino T, Mizushima J, Hori H Nishino T (2000) Sequence motif-specific assignment of two [2Fe-2S] clusters in rat xanthine oxidoreductase studied by site-directed mutagenesis. J Biochem (Tokyo) 127, 771 778.
    • (2000) J Biochem (Tokyo) , vol.127 , pp. 771-778
    • Iwasaki, T.1    Okamoto, K.2    Nishino, T.3    Mizushima, J.4    Hori, H.5    Nishino, T.6
  • 59
    • 0026806101 scopus 로고
    • Purification and properties of milk xanthine dehydrogenase
    • Hunt J Massey V (1992) Purification and properties of milk xanthine dehydrogenase. J Biol Chem 267, 21479 21485.
    • (1992) J Biol Chem , vol.267 , pp. 21479-21485
    • Hunt, J.1    Massey, V.2
  • 60
    • 0027209264 scopus 로고
    • Redox potentials of milk xanthine dehydrogenase. Room temperature measurement of the FAD and 2Fe/2S center potentials
    • Hunt J, Massey V, Dunham WR Sands RH (1993) Redox potentials of milk xanthine dehydrogenase. Room temperature measurement of the FAD and 2Fe/2S center potentials. J Biol Chem 268, 18685 18691.
    • (1993) J Biol Chem , vol.268 , pp. 18685-18691
    • Hunt, J.1    Massey, V.2    Dunham, W.R.3    Sands, R.H.4
  • 61
    • 0024556882 scopus 로고
    • The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. Evidence for alteration of the redox potential of the flavin by NAD binding or modification of the NAD-binding site and isolation of a modified peptide
    • Nishino T Nishino T (1989) The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. Evidence for alteration of the redox potential of the flavin by NAD binding or modification of the NAD-binding site and isolation of a modified peptide. J Biol Chem 264, 5468 5473.
    • (1989) J Biol Chem , vol.264 , pp. 5468-5473
    • Nishino, T.1    Nishino, T.2
  • 62
    • 0030716904 scopus 로고    scopus 로고
    • The oxidative half-reaction of xanthine dehydrogenase with NAD; Reaction kinetics and steady-state mechanism
    • Harris CM Massey V (1997) The oxidative half-reaction of xanthine dehydrogenase with NAD; reaction kinetics and steady-state mechanism. J Biol Chem 272, 28335 28341.
    • (1997) J Biol Chem , vol.272 , pp. 28335-28341
    • Harris, C.M.1    Massey, V.2
  • 63
    • 0024586608 scopus 로고
    • The reactivity of chicken liver xanthine dehydrogenase with molecular oxygen
    • Nishino T, Nishino T, Schopfer LM Massey V (1989) The reactivity of chicken liver xanthine dehydrogenase with molecular oxygen. J Biol Chem 264, 2518 2527.
    • (1989) J Biol Chem , vol.264 , pp. 2518-2527
    • Nishino, T.1    Nishino, T.2    Schopfer, L.M.3    Massey, V.4
  • 64
    • 0019877327 scopus 로고
    • Studies on the oxidative half-reaction of xanthine oxidase
    • Hille R Massey V (1981) Studies on the oxidative half-reaction of xanthine oxidase. J Biol Chem 256, 9090 9095.
    • (1981) J Biol Chem , vol.256 , pp. 9090-9095
    • Hille, R.1    Massey, V.2
  • 65
    • 0024508870 scopus 로고
    • Reactivity of chicken liver xanthine dehydrogenase containing modified flavins
    • Nishino T, Nishino T, Schopfer LM Massey V (1989) Reactivity of chicken liver xanthine dehydrogenase containing modified flavins. J Biol Chem 264, 6075 6085.
    • (1989) J Biol Chem , vol.264 , pp. 6075-6085
    • Nishino, T.1    Nishino, T.2    Schopfer, L.M.3    Massey, V.4
  • 66
    • 0024452395 scopus 로고
    • 2-dependent types of rat liver xanthine dehydrogenase shown by active site probe study
    • 2-dependent types of rat liver xanthine dehydrogenase shown by active site probe study. J Biol Chem 264, 15930 15935.
    • (1989) J Biol Chem , vol.264 , pp. 15930-15935
    • Saito, T.1    Nishino, T.2    Massey, V.3
  • 67
    • 0024349097 scopus 로고
    • Differences in protein structure of xanthine dehydrogenase and xanthine oxidase revealed by reconstitution with flavin active site probes
    • Massey V, Schopfer LM, Nishino T Nishino T (1989) Differences in protein structure of xanthine dehydrogenase and xanthine oxidase revealed by reconstitution with flavin active site probes. J Biol Chem 264, 10567 10573.
    • (1989) J Biol Chem , vol.264 , pp. 10567-10573
    • Massey, V.1    Schopfer, L.M.2    Nishino, T.3    Nishino, T.4
  • 68
    • 0018787230 scopus 로고
    • Properties of flavins where the 8-methyl group is replaced by mercapto- residues
    • Moore EG, Ghisla S Massey V (1979) Properties of flavins where the 8-methyl group is replaced by mercapto- residues. J Biol Chem 254, 8173 8178.
    • (1979) J Biol Chem , vol.254 , pp. 8173-8178
    • Moore, E.G.1    Ghisla, S.2    Massey, V.3
  • 69
    • 0022800854 scopus 로고
    • New flavins for old: Artificial flavins as active site probes of flavoproteins
    • Ghisla S Massey V (1986) New flavins for old: artificial flavins as active site probes of flavoproteins. Biochem J 239, 1 12.
    • (1986) Biochem J , vol.239 , pp. 1-12
    • Ghisla, S.1    Massey, V.2
  • 70
    • 0014788052 scopus 로고
    • The chemical and electronic structure of the neutral flavin radical as revealed by electron spin resonance spectroscopy of chemically and isotopically substituted derivatives
    • Muller F, Hemmerich P, Ehrenberg A, Palmer G Massey V (1970) The chemical and electronic structure of the neutral flavin radical as revealed by electron spin resonance spectroscopy of chemically and isotopically substituted derivatives. Eur J Biochem 14, 185 196.
    • (1970) Eur J Biochem , vol.14 , pp. 185-196
    • Muller, F.1    Hemmerich, P.2    Ehrenberg, A.3    Palmer, G.4    Massey, V.5
  • 71
    • 0002989674 scopus 로고
    • 2-dependent types of rat liver xanthine dehydrogenase
    • 2- dependent types of rat liver xanthine dehydrogenase. Yokohama Med Bull 38, 151 168.
    • (1987) Yokohama Med Bull , vol.38 , pp. 151-168
    • Saito, T.1
  • 72
    • 0030693643 scopus 로고    scopus 로고
    • The conversion from the dehydrogenase type to the oxidase type of rat liver xanthine dehydrogenase by modification of cysteine residues with fluorodinitrobenzene
    • Nishino T Nishino T (1997) The conversion from the dehydrogenase type to the oxidase type of rat liver xanthine dehydrogenase by modification of cysteine residues with fluorodinitrobenzene. J Biol Chem 272, 29859 29864.
    • (1997) J Biol Chem , vol.272 , pp. 29859-29864
    • Nishino, T.1    Nishino, T.2
  • 74
    • 0028893185 scopus 로고
    • The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure
    • Sato A, Nishino T, Noda K, Amaya Y Nishino T (1995) The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure. J Biol Chem 270, 2818 2826.
    • (1995) J Biol Chem , vol.270 , pp. 2818-2826
    • Sato, A.1    Nishino, T.2    Noda, K.3    Amaya, Y.4    Nishino, T.5
  • 75
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym O Eisenberg D (2001) Sequence-structure analysis of FAD-containing proteins. Protein Sci 10, 1712 1728.
    • (2001) Protein Sci , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 76
    • 0034645779 scopus 로고    scopus 로고
    • Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: Gated substrate entry and proton relays support the proposed catalytic mechanism
    • Cunane LM, Chen ZW, Shamala N, Mathews FS, Cronin CN McIntire WS (2000) Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism. J Mol Biol 295, 357 374.
    • (2000) J Mol Biol , vol.295 , pp. 357-374
    • Cunane, L.M.1    Chen, Z.W.2    Shamala, N.3    Mathews, F.S.4    Cronin, C.N.5    McIntire, W.S.6
  • 79
    • 44949208442 scopus 로고    scopus 로고
    • The mechanism of transition from xanthine dehydrogenase to xanthine oxidase: Effect of guanidine-HCl or urea on the activity
    • in press).
    • Tsujii A Nishino T (2008) The mechanism of transition from xanthine dehydrogenase to xanthine oxidase: effect of guanidine-HCl or urea on the activity. Nucleoside, Nucleotide Nucleic Acid (in press).
    • (2008) Nucleoside, Nucleotide Nucleic Acid
    • Tsujii, A.1    Nishino, T.2


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