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Volumn 109, Issue 37, 2012, Pages 14773-14778

Pyranopterin conformation defines the function of molybdenum and tungsten enzymes

Author keywords

Energetics; Molybdoenzymes; Redox chemistry

Indexed keywords

DIMETHYL SULFOXIDE REDUCTASE; ENZYME; MOLYBDENUM; MOLYBDENUM ENZYME; PYRANOPTERIN; QUINONE DERIVATIVE; SULFITE OXIDASE; TUNGSTEN; TUNGSTEN ENZYME; UNCLASSIFIED DRUG; XANTHINE DEHYDROGENASE;

EID: 84866284890     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1200671109     Document Type: Article
Times cited : (87)

References (38)
  • 2
    • 65949088825 scopus 로고    scopus 로고
    • Molybdenum and tungsten enzymes: A crystallographic and mechanistic overview
    • Romao MJ (2009) Molybdenum and tungsten enzymes: A crystallographic and mechanistic overview. Dalton Trans 4053-4068.
    • (2009) Dalton Trans , pp. 4053-4068
    • Romao, M.J.1
  • 3
    • 0036365692 scopus 로고    scopus 로고
    • Molybdenum enzymes containing the pyranopterin cofactor: An overview
    • Hille R (2002) Molybdenum enzymes containing the pyranopterin cofactor: An overview. Met Ions Biol Syst 39:187-226.
    • (2002) Met Ions Biol Syst , vol.39 , pp. 187-226
    • Hille, R.1
  • 4
    • 68949107281 scopus 로고    scopus 로고
    • Molybdenum cofactors, enzymes and pathways
    • Schwarz G, Mendel RR, Ribbe MW (2009) Molybdenum cofactors, enzymes and pathways. Nature 460:839-847.
    • (2009) Nature , vol.460 , pp. 839-847
    • Schwarz, G.1    Mendel, R.R.2    Ribbe, M.W.3
  • 5
    • 44949191540 scopus 로고    scopus 로고
    • Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold
    • Workun GJ, Moquin K, Rothery RA, Weiner JH (2008) Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold. Microbiol Mol Biol Rev 72:228-248.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 228-248
    • Workun, G.J.1    Moquin, K.2    Rothery, R.A.3    Weiner, J.H.4
  • 6
    • 79952764486 scopus 로고    scopus 로고
    • Spectroscopic studies of molybdenum and tungsten enzymes
    • Pushie MJ, George GN (2011) Spectroscopic studies of molybdenum and tungsten enzymes. Coord Chem Rev 255:1055-1084.
    • (2011) Coord Chem Rev , vol.255 , pp. 1055-1084
    • Pushie, M.J.1    George, G.N.2
  • 7
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267:1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 8
    • 79959508404 scopus 로고    scopus 로고
    • Spectroscopic and electronic structure studies of a dimethyl sulfoxide reductase catalytic intermediate: Implications for electron- and atom-transfer reactivity
    • Mtei RP, et al. (2011) Spectroscopic and electronic structure studies of a dimethyl sulfoxide reductase catalytic intermediate: Implications for electron- and atom-transfer reactivity. J Am Chem Soc 133:9762-9774.
    • (2011) J Am Chem Soc , vol.133 , pp. 9762-9774
    • Mtei, R.P.1
  • 9
    • 77953300772 scopus 로고    scopus 로고
    • Noninnocent dithiolene ligands: A new oxomolybdenum complex possessing a donor-acceptor dithiolene ligand
    • Matz KG, Mtei RP, Leung B, Burgmayer SJN, Kirk ML (2010) Noninnocent dithiolene ligands: A new oxomolybdenum complex possessing a donor-acceptor dithiolene ligand. J Am Chem Soc 132:7830-7831.
    • (2010) J Am Chem Soc , vol.132 , pp. 7830-7831
    • Matz, K.G.1    Mtei, R.P.2    Leung, B.3    Burgmayer, S.J.N.4    Kirk, M.L.5
  • 10
    • 0035944487 scopus 로고    scopus 로고
    • Thermally driven intramolecular charge transfer in an oxo-molybdenum dithiolate complex
    • Helton ME, et al. (2001) Thermally driven intramolecular charge transfer in an oxo-molybdenum dithiolate complex. J Am Chem Soc 123:10389-10390.
    • (2001) J Am Chem Soc , vol.123 , pp. 10389-10390
    • Helton, M.E.1
  • 11
    • 83755183544 scopus 로고    scopus 로고
    • A valence bond description of dizwitterionic dithiolene character in an oxomolybdenum-bis(dithione) complex
    • in press
    • Mtei RP, et al. (2011) A valence bond description of dizwitterionic dithiolene character in an oxomolybdenum-bis(dithione) complex. Eur J Inorg Chem, in press.
    • (2011) Eur J Inorg Chem
    • Mtei, R.P.1
  • 13
    • 79952762443 scopus 로고    scopus 로고
    • Pterin chemistry and its relationship to the molybdenum cofactor
    • Basu P, Burgmayer SJN (2011) Pterin chemistry and its relationship to the molybdenum cofactor. Coord Chem Rev 255:1016-1038.
    • (2011) Coord Chem Rev , vol.255 , pp. 1016-1038
    • Basu, P.1    Burgmayer, S.J.N.2
  • 14
    • 80053939699 scopus 로고    scopus 로고
    • Study of molybdenum(4+) quinoxalyldithiolenes as models for the noninnocent pyranopterin in the molybdenum cofactor
    • Matz KG, Mtei RP, Rothstein R, Kirk ML, Burgmayer SJN (2011) Study of molybdenum(4+) quinoxalyldithiolenes as models for the noninnocent pyranopterin in the molybdenum cofactor. Inorg Chem 50:9804-9815.
    • (2011) Inorg Chem , vol.50 , pp. 9804-9815
    • Matz, K.G.1    Mtei, R.P.2    Rothstein, R.3    Kirk, M.L.4    Burgmayer, S.J.N.5
  • 15
    • 0031447054 scopus 로고    scopus 로고
    • The coordination chemistry and function of the molybdenum centres of the oxomolybdoenzymes
    • Enemark JH, Garner CD (1997) The coordination chemistry and function of the molybdenum centres of the oxomolybdoenzymes. J Biol Inorg Chem 2:817-822.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 817-822
    • Enemark, J.H.1    Garner, C.D.2
  • 16
    • 0001630824 scopus 로고    scopus 로고
    • The relative stabilities of dihydropterins; a comment on the structureof Moco, the cofactor of the oxomolybdoenzymes
    • Greatbanks SP, Hillier IH, Garner CD, Joule JA (1997) The relative stabilities of dihydropterins; a comment on the structureof Moco, the cofactor of the oxomolybdoenzymes. J Chem Soc Perkin Trans 2:1529-1534.
    • (1997) J Chem Soc Perkin Trans , vol.2 , pp. 1529-1534
    • Greatbanks, S.P.1    Hillier, I.H.2    Garner, C.D.3    Joule, J.A.4
  • 17
    • 37049103095 scopus 로고
    • Pterins. Part 9. The structure of quinonoid dihydropterins [2-amino-7,8-dihydropteridin-4(6H)-ones]
    • Armarego WLF, Waring P (1982) Pterins. Part 9. The structure of quinonoid dihydropterins [2-amino-7,8-dihydropteridin-4(6H)-ones]. J Chem Soc Perkin Trans 2:1227-1233.
    • (1982) J Chem Soc Perkin Trans , vol.2 , pp. 1227-1233
    • Armarego, W.L.F.1    Waring, P.2
  • 18
    • 33748296263 scopus 로고    scopus 로고
    • Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum
    • Kloer DP, Hagel C, Heider J, Schulz GE (2006) Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum. Structure 14:1377-1388.
    • (2006) Structure , vol.14 , pp. 1377-1388
    • Kloer, D.P.1    Hagel, C.2    Heider, J.3    Schulz, G.E.4
  • 19
    • 0041318860 scopus 로고    scopus 로고
    • Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
    • Bertero MG, et al. (2003) Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat Struct Biol 10:681-687.
    • (2003) Nat Struct Biol , vol.10 , pp. 681-687
    • Bertero, M.G.1
  • 20
    • 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
  • 21
    • 0025356250 scopus 로고
    • The state of reduction of molybdopterin in xanthine oxidase and sulfite oxidase
    • Gardlik S, Rajagopalan KV (1990) The state of reduction of molybdopterin in xanthine oxidase and sulfite oxidase. J Biol Chem 265:13047-13054.
    • (1990) J Biol Chem , vol.265 , pp. 13047-13054
    • Gardlik, S.1    Rajagopalan, K.V.2
  • 22
    • 0025819334 scopus 로고
    • Oxidation of molybdopterin in sulfite oxidase by ferricyanide effect on electron transfer activities
    • Gardlik S, Rajagopalan KV (1991) Oxidation of molybdopterin in sulfite oxidase by ferricyanide effect on electron transfer activities. J Biol Chem 266:4889-4895.
    • (1991) J Biol Chem , vol.266 , pp. 4889-4895
    • Gardlik, S.1    Rajagopalan, K.V.2
  • 23
    • 0346481618 scopus 로고
    • Studies on the oxidation state of molybdopterin
    • Rajagopalan KV, Kramer S, Gardlik S (1986) Studies on the oxidation state of molybdopterin. Polyhedron 5:573-576.
    • (1986) Polyhedron , vol.5 , pp. 573-576
    • Rajagopalan, K.V.1    Kramer, S.2    Gardlik, S.3
  • 24
    • 50049103112 scopus 로고    scopus 로고
    • The prokaryotic complex iron-sulfur molybdoenzyme family
    • Rothery RA, Workun GJ, Weiner JH (2008) The prokaryotic complex iron-sulfur molybdoenzyme family. Biochim Biophys Acta 1778:1897-1929.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1897-1929
    • Rothery, R.A.1    Workun, G.J.2    Weiner, J.H.3
  • 25
    • 79955478107 scopus 로고    scopus 로고
    • The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states
    • Coelho C, et al. (2011) The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states. J Mol Biol 408:932-948.
    • (2011) J Mol Biol , vol.408 , pp. 932-948
    • Coelho, C.1
  • 26
    • 0014775290 scopus 로고
    • Reduction potentials of tetrahydropterins
    • Archer MC, Scrimgeour KG (1970) Reduction potentials of tetrahydropterins. Can J Biochem 48:526-527.
    • (1970) Can J Biochem , vol.48 , pp. 526-527
    • Archer, M.C.1    Scrimgeour, K.G.2
  • 27
    • 0001553122 scopus 로고
    • Induced internal redox processes in molybdenum-sulfur chemistry: Conversion of tetrathiomolybdate(2-) ion to octathiodimolybdate(2-) ion by organic disulfides
    • Pan WH, Harmer MA, Halbert TR, Stiefel EI (1984) Induced internal redox processes in molybdenum-sulfur chemistry: Conversion of tetrathiomolybdate(2-) ion to octathiodimolybdate(2-) ion by organic disulfides. J Am Chem Soc 106:459-460.
    • (1984) J Am Chem Soc , vol.106 , pp. 459-460
    • Pan, W.H.1    Harmer, M.A.2    Halbert, T.R.3    Stiefel, E.I.4
  • 28
    • 0001453468 scopus 로고
    • Synthesis of cyclopentadiemnyk-ene-1,2-dithiolatocobalt complexes and coupled proton-electron transfer in a substituted quinaxalinyl derivatives
    • David Garner C, et al. (1993) Synthesis of cyclopentadiemnyk-ene-1,2- dithiolatocobalt complexes and coupled proton-electron transfer in a substituted quinaxalinyl derivatives. Heterocycles 35:563-568.
    • (1993) Heterocycles , vol.35 , pp. 563-568
    • David Garner, C.1
  • 29
    • 33745933654 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis and molybdenum enzymes
    • Schwarz G, Mendel RR (2006) Molybdenum cofactor biosynthesis and molybdenum enzymes. Annu Rev Plant Biol 57:623-647.
    • (2006) Annu Rev Plant Biol , vol.57 , pp. 623-647
    • Schwarz, G.1    Mendel, R.R.2
  • 30
    • 16244366777 scopus 로고    scopus 로고
    • Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites
    • Armstrong FA (2005) Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites. Curr Opin Chem Biol 9:110-117.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 110-117
    • Armstrong, F.A.1
  • 31
    • 0035852958 scopus 로고    scopus 로고
    • Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway
    • Heffron K, Léger C, Rothery RA, Weiner JH, Armstrong FA (2001) Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway. Biochemistry 40:3117-3126.
    • (2001) Biochemistry , vol.40 , pp. 3117-3126
    • Heffron, K.1    Léger, C.2    Rothery, R.A.3    Weiner, J.H.4    Armstrong, F.A.5
  • 32
    • 0031593019 scopus 로고    scopus 로고
    • Active site structures and catalytic mechanism of Rhodobacter sphaeroides dimethyl sulfoxide reductase as revealed by Resonance Raman spectroscopy
    • Garton SD, et al. (1997) Active site structures and catalytic mechanism of Rhodobacter sphaeroides dimethyl sulfoxide reductase as revealed by Resonance Raman spectroscopy. J Am Chem Soc 119:12906-12916.
    • (1997) J Am Chem Soc , vol.119 , pp. 12906-12916
    • Garton, S.D.1
  • 33
    • 0034629467 scopus 로고    scopus 로고
    • Resonance Raman characterization of biotin sulfoxide reductase Comparing oxomolybdenum enzymes in the ME(2)SO reductase family
    • Garton SD, et al. (2000) Resonance Raman characterization of biotin sulfoxide reductase Comparing oxomolybdenum enzymes in the ME(2)SO reductase family. J Biol Chem 275:6798-6805.
    • (2000) J Biol Chem , vol.275 , pp. 6798-6805
    • Garton, S.D.1
  • 34
    • 0030897597 scopus 로고    scopus 로고
    • Resonance Raman characterization of the molybdenum center in sulfite oxidase: Identification of MoO stretching modes
    • Garton SD, Garrett RM, Rajagopalan KV, Johnson MK (1997) Resonance Raman characterization of the molybdenum center in sulfite oxidase: Identification of MoO stretching modes. J Am Chem Soc 119:2590-2591.
    • (1997) J Am Chem Soc , vol.119 , pp. 2590-2591
    • Garton, S.D.1    Garrett, R.M.2    Rajagopalan, K.V.3    Johnson, M.K.4
  • 35
    • 77954724481 scopus 로고    scopus 로고
    • Three-dimensional structural model of chicken liver sulfite oxidase in its activated form
    • Utesch T, Mroginski MA (2010) Three-dimensional structural model of chicken liver sulfite oxidase in its activated form. J Phys Chem Lett 1:2159-2164.
    • (2010) J Phys Chem Lett , vol.1 , pp. 2159-2164
    • Utesch, T.1    Mroginski, M.A.2
  • 36
    • 77749316072 scopus 로고    scopus 로고
    • Active-site dynamics and large-scale domain motions of sulfite oxidase: A molecular dynamics study
    • Pushie MJ, George GN (2010) Active-site dynamics and large-scale domain motions of sulfite oxidase: A molecular dynamics study. J Phys Chem B 114:3266-3275.
    • (2010) J Phys Chem B , vol.114 , pp. 3266-3275
    • Pushie, M.J.1    George, G.N.2
  • 37
    • 79952764690 scopus 로고    scopus 로고
    • Structural aspects of mononuclear Mo/W-enzymes
    • Holger D (2011) Structural aspects of mononuclear Mo/W-enzymes. Coord Chem Rev 255:1104-1116.
    • (2011) Coord Chem Rev , vol.255 , pp. 1104-1116
    • Holger, D.1
  • 38
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60:2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


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