메뉴 건너뛰기




Volumn 47, Issue 43, 2008, Pages 11168-11170

Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase

Author keywords

[No Author keywords available]

Indexed keywords

OXYGEN; POWDERS;

EID: 54849437492     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801459q     Document Type: Article
Times cited : (51)

References (17)
  • 1
    • 0001615959 scopus 로고
    • Mechanistic aspects of dihydroxybenzoate dioxygenases
    • Lipscomb, J. D., and Orville, A. M. (1992) Mechanistic aspects of dihydroxybenzoate dioxygenases. Metal Ions Biol. Syst. 28, 243-298.
    • (1992) Metal Ions Biol. Syst , vol.28 , pp. 243-298
    • Lipscomb, J.D.1    Orville, A.M.2
  • 4
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
    • Han, S., Eltis, L. D., Timmis, K. N., Muchmore, S. W., and Bolin, J. T. (1995) Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270, 976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 5
    • 0002955249 scopus 로고
    • Three-dimensional structure of 2,3-dihydroxybiphenyl dioxygenase (BphC enzyme) from Pseudomonas sp. strain KKS102 having polychlorinated biphenyl (PCB)-degrading activity
    • Sugiyama, K., Senda, T., Narita, H., Yamamoto, T., Kimbara, K., Fukuda, M., Yano, K., and Mitsui, Y. (1995) Three-dimensional structure of 2,3-dihydroxybiphenyl dioxygenase (BphC enzyme) from Pseudomonas sp. strain KKS102 having polychlorinated biphenyl (PCB)-degrading activity. Proc. Jpn. Acad., Ser. B 71, 32-35.
    • (1995) Proc. Jpn. Acad., Ser. B , vol.71 , pp. 32-35
    • Sugiyama, K.1    Senda, T.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Yano, K.7    Mitsui, Y.8
  • 6
    • 1642264726 scopus 로고    scopus 로고
    • Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases
    • Vetting, M. W., Wackett, L. P., Que, L., Jr., Lipscomb, J. D., and Ohlendorf, D. H. (2004) Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J. Bacteriol. 186, 1945-1958.
    • (2004) J. Bacteriol , vol.186 , pp. 1945-1958
    • Vetting, M.W.1    Wackett, L.P.2    Que Jr., L.3    Lipscomb, J.D.4    Ohlendorf, D.H.5
  • 9
    • 0043022281 scopus 로고    scopus 로고
    • Dioxygenase enzymes: Catalytic mechanisms and chemical models
    • Bugg, T. D. H. (2003) Dioxygenase enzymes: Catalytic mechanisms and chemical models. Tetrahedron 59, 7075-7101.
    • (2003) Tetrahedron , vol.59 , pp. 7075-7101
    • Bugg, T.D.H.1
  • 10
    • 0038627547 scopus 로고    scopus 로고
    • A density functional investigation of the extradiol cleavage mechanism in non-heme iron catechol dioxygenases
    • Deeth, R. J., and Bugg, T. D. H. (2003) A density functional investigation of the extradiol cleavage mechanism in non-heme iron catechol dioxygenases. J. Biol. Inorg. Chem. 8, 409-418.
    • (2003) J. Biol. Inorg. Chem , vol.8 , pp. 409-418
    • Deeth, R.J.1    Bugg, T.D.H.2
  • 11
    • 3242811958 scopus 로고    scopus 로고
    • Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases
    • Siegbahn, P. E. M., and Haeffner, F. (2004) Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases. J. Am. Chem. Soc. 126, 8919-8932.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8919-8932
    • Siegbahn, P.E.M.1    Haeffner, F.2
  • 12
    • 39449130475 scopus 로고    scopus 로고
    • Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
    • Kovaleva, E. G., and Lipscomb, J. D. (2008) Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat. Chem. Biol. 4, 186-193.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 186-193
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 13
    • 44949225065 scopus 로고    scopus 로고
    • Swapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox state
    • Emerson, J. P., Kovaleva, E. G., Farquhar, E. R., Lipscomb, J. D., and Que, L., Jr. (2008) Swapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox state. Proc. Natl. Acad. Sci. U.S.A. 105, 7347-7352.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 7347-7352
    • Emerson, J.P.1    Kovaleva, E.G.2    Farquhar, E.R.3    Lipscomb, J.D.4    Que Jr., L.5
  • 14
    • 18544362332 scopus 로고    scopus 로고
    • Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: Role of His200 in the kinetics of interconversion of reaction cycle intermediates
    • Groce, S. L., and Lipscomb, J. D. (2005) Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: Role of His200 in the kinetics of interconversion of reaction cycle intermediates. Biochemistry 44, 7175-7188.
    • (2005) Biochemistry , vol.44 , pp. 7175-7188
    • Groce, S.L.1    Lipscomb, J.D.2
  • 15
    • 10044256407 scopus 로고    scopus 로고
    • Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
    • Groce, S. L., Miller-Rodeberg, M. A., and Lipscomb, J. D. (2004) Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase. Biochemistry 43, 15141-15153.
    • (2004) Biochemistry , vol.43 , pp. 15141-15153
    • Groce, S.L.1    Miller-Rodeberg, M.A.2    Lipscomb, J.D.3
  • 16
    • 34247534094 scopus 로고    scopus 로고
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science 316, 453-457.
    • (2007) Science , vol.316 , pp. 453-457
    • Kovaleva, E.G.1    Lipscomb, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.