메뉴 건너뛰기




Volumn 51, Issue 44, 2012, Pages 8743-8754

Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: Intermediates formed by a tyrosine 257 variant

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AROMATIC RINGS; AROMATIC SUBSTRATES; CATALYTIC CYCLES; ELECTRON DELOCALIZATION; ELECTRON TRANSFER; MOSSBAUER; OXYGEN ACTIVATIONS; SEMIQUINONES; STOPPED-FLOW STUDIES; TRANSIENT KINETIC ANALYSIS;

EID: 84868584569     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301114x     Document Type: Article
Times cited : (37)

References (33)
  • 1
    • 0029883485 scopus 로고    scopus 로고
    • Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum - A dioxygenase with catalase activity
    • Miller, M. A. and Lipscomb, J. D. (1996) Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum-A dioxygenase with catalase activity J. Biol. Chem. 271, 5524-5535
    • (1996) J. Biol. Chem. , vol.271 , pp. 5524-5535
    • Miller, M.A.1    Lipscomb, J.D.2
  • 2
    • 84868537748 scopus 로고    scopus 로고
    • Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation
    • DOI: 10.1021/bi301115c
    • Kovaleva, E. G. and Lipscomb, J. D. Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation. Biochemistry 2012, 51, DOI: 10.1021/bi301115c.
    • (2012) Biochemistry , vol.51
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 3
    • 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
  • 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
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102
    • Senda, T., Sugiyama, K., Narita, H., Yamamoto, T., Kimbara, K., Fukuda, M., Sato, M., Yano, K., and Mitsui, Y. (1996) Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102 J. Mol. Biol. 255, 735-752
    • (1996) J. Mol. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Sugiyama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 6
    • 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
  • 7
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • Hegg, E. L. and Que, L. (1997) The 2-His-1-carboxylate facial triad: An emerging structural motif in mononuclear non-heme iron(II) enzymes Eur. J. Biochem. 250, 625-629
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que, L.2
  • 8
    • 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
  • 9
    • 0037139492 scopus 로고    scopus 로고
    • Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/vis absorption spectroscopy, and crystallography
    • Vaillancourt, F. H., Barbosa, C. J., Spiro, T. G., Bolin, J. T., Blades, M. W., Turner, R. F. B., and Eltis, L. D. (2002) Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/vis absorption spectroscopy, and crystallography J. Am. Chem. Soc. 124, 2485-2496
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2485-2496
    • Vaillancourt, F.H.1    Barbosa, C.J.2    Spiro, T.G.3    Bolin, J.T.4    Blades, M.W.5    Turner, R.F.B.6    Eltis, L.D.7
  • 11
    • 57049146277 scopus 로고    scopus 로고
    • Mechanism of extradiol aromatic ring-cleaving dioxygenases
    • Lipscomb, J. D. (2008) Mechanism of extradiol aromatic ring-cleaving dioxygenases Curr. Opin. Struct. Biol. 18, 644-649
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 644-649
    • Lipscomb, J.D.1
  • 12
    • 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
  • 14
    • 84855836967 scopus 로고    scopus 로고
    • Non-heme iron-dependent dioxygenases: Mechanism and structure
    • (de Visser, S. P. and Kumar, D. Eds.) pp, The Royal Society of Chemistry, Cambridge, UK
    • Bugg, T. D. H. (2011) Non-heme iron-dependent dioxygenases: Mechanism and structure, In Iron-Containing Enzymes: Versatile Catalysts of Hydroxylation Reactions in Nature (de Visser, S. P. and Kumar, D., Eds.) pp 42-66, The Royal Society of Chemistry, Cambridge, UK.
    • (2011) Iron-Containing Enzymes: Versatile Catalysts of Hydroxylation Reactions in Nature , pp. 42-66
    • Bugg, T.D.H.1
  • 15
    • 54849437492 scopus 로고    scopus 로고
    • Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase
    • Kovaleva, E. G. and Lipscomb, J. D. (2008) Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase Biochemistry 47, 11168-11170
    • (2008) Biochemistry , vol.47 , pp. 11168-11170
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 18
    • 0027454094 scopus 로고
    • Transient intermediates of the methane monooxygenase catalytic cycle
    • Lee, S. K., Nesheim, J. C., and Lipscomb, J. D. (1993) Transient intermediates of the methane monooxygenase catalytic cycle J. Biol. Chem. 268, 21569-21577
    • (1993) J. Biol. Chem. , vol.268 , pp. 21569-21577
    • Lee, S.K.1    Nesheim, J.C.2    Lipscomb, J.D.3
  • 19
    • 0002822447 scopus 로고    scopus 로고
    • 57Fe Mössbauer spectroscopy
    • (Que, L. Jr. Ed.) pp, University Science Books, Sausalito, CA
    • 57Fe Mössbauer spectroscopy, in Physical Methods in Bioinorganic Chemistry (Que, L., Jr., Ed.) pp 287-319, University Science Books, Sausalito, CA.
    • (2000) Physical Methods in Bioinorganic Chemistry , pp. 287-319
    • Münck, E.1
  • 20
    • 0016284228 scopus 로고
    • Dopaquinone and related compounds. Reactions with o-phenylenediamine
    • Omote, Y., Hirama, T., and Komatsu, T. (1974) Dopaquinone and related compounds. Reactions with o-phenylenediamine Bull. Chem. Soc. Jpn. 47, 1957-1959
    • (1974) Bull. Chem. Soc. Jpn. , vol.47 , pp. 1957-1959
    • Omote, Y.1    Hirama, T.2    Komatsu, T.3
  • 21
    • 33847086663 scopus 로고
    • Iron(III), manganese(III), and cobalt(III) complexes with single chelating o-semiquinone ligands
    • Kessel, S. L., Emberson, R. M., Debrunner, P. G., and Hendrickson, D. N. (1980) Iron(III), manganese(III), and cobalt(III) complexes with single chelating o-semiquinone ligands Inorg. Chem. 19, 1170-1178
    • (1980) Inorg. Chem. , vol.19 , pp. 1170-1178
    • Kessel, S.L.1    Emberson, R.M.2    Debrunner, P.G.3    Hendrickson, D.N.4
  • 22
    • 0008268720 scopus 로고
    • High field Mössbauer studies of reduced protocatechuate 3,4 dioxygenase
    • Zimmermann, R., Huynh, B. H., Münck, E., and Lipscomb, J. D. (1978) High field Mössbauer studies of reduced protocatechuate 3,4 dioxygenase J. Chem. Phys. 69, 5463-5467
    • (1978) J. Chem. Phys. , vol.69 , pp. 5463-5467
    • Zimmermann, R.1    Huynh, B.H.2    Münck, E.3    Lipscomb, J.D.4
  • 23
    • 1842637848 scopus 로고    scopus 로고
    • CD and MCD studies of the non-heme ferrous active site in (4-hydroxyphenyl)pyruvate dioxygenase: Correlation between oxygen activation in the extradiol and alpha -KG-dependent dioxygenases
    • Neidig, M. L., Kavana, M., Moran, G. R., and Solomon, E. I. (2004) CD and MCD studies of the non-heme ferrous active site in (4-hydroxyphenyl)pyruvate dioxygenase: Correlation between oxygen activation in the extradiol and alpha -KG-dependent dioxygenases J. Am. Chem. Soc. 126, 4486-4487
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4486-4487
    • Neidig, M.L.1    Kavana, M.2    Moran, G.R.3    Solomon, E.I.4
  • 24
    • 84987082395 scopus 로고
    • Properties of a 5T2 in iron (II) under the action of arbitrary-symmetry ligand fields and spin-orbit coupling I. on the quadrupole splitting
    • Zimmermann, R. and Spiering, H. (1975) Properties of a 5T2 in iron (II) under the action of arbitrary-symmetry ligand fields and spin-orbit coupling I. On the quadrupole splitting Phys. Status Solidi 67, 487-494
    • (1975) Phys. Status Solidi , vol.67 , pp. 487-494
    • Zimmermann, R.1    Spiering, H.2
  • 25
    • 0141732267 scopus 로고    scopus 로고
    • Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme
    • Groce, S. L. and Lipscomb, J. D. (2003) Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme J. Am. Chem. Soc. 125, 11780-11781
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11780-11781
    • Groce, S.L.1    Lipscomb, J.D.2
  • 26
    • 0032562027 scopus 로고    scopus 로고
    • 3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: Evidence for new reaction cycle intermediates
    • 3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates Biochemistry 37, 2131-2144
    • (1998) Biochemistry , vol.37 , pp. 2131-2144
    • Frazee, R.W.1    Orville, A.M.2    Dolbeare, K.B.3    Yu, H.4    Ohlendorf, D.H.5    Lipscomb, J.D.6
  • 27
    • 23944461020 scopus 로고    scopus 로고
    • Roles of the equatorial tyrosyl iron ligand of protocatechuate 3,4-dioxygenase in catalysis
    • Valley, M. P., Brown, C. K., Burk, D. L., Vetting, M. W., Ohlendorf, D. H., and Lipscomb, J. D. (2005) Roles of the equatorial tyrosyl iron ligand of protocatechuate 3,4-dioxygenase in catalysis Biochemistry 44, 11024-11039
    • (2005) Biochemistry , vol.44 , pp. 11024-11039
    • Valley, M.P.1    Brown, C.K.2    Burk, D.L.3    Vetting, M.W.4    Ohlendorf, D.H.5    Lipscomb, J.D.6
  • 29
    • 0000006176 scopus 로고
    • Variable-temperature variable-field magnetic circular dichroism studies of the iron(II) active site in metapyrocatechase: Implications for the molecular mechanism of extradiol dioxygenases
    • Mabrouk, P. A., Orville, A. M., Lipscomb, J. D., and Solomon, E. I. (1991) Variable-temperature variable-field magnetic circular dichroism studies of the iron(II) active site in metapyrocatechase: implications for the molecular mechanism of extradiol dioxygenases J. Am. Chem. Soc. 113, 4053-4061
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4053-4061
    • Mabrouk, P.A.1    Orville, A.M.2    Lipscomb, J.D.3    Solomon, E.I.4
  • 30
    • 0034828607 scopus 로고    scopus 로고
    • Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities
    • Zhou, J., Kelly, W. L., Bachmann, B. O., Gunsior, M., Townsend, C. A., and Solomon, E. I. (2001) Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities J. Am. Chem. Soc. 123, 7388-7398
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7388-7398
    • Zhou, J.1    Kelly, W.L.2    Bachmann, B.O.3    Gunsior, M.4    Townsend, C.A.5    Solomon, E.I.6
  • 31
    • 0035898074 scopus 로고    scopus 로고
    • Geometric and electronic structure contributions to function in bioinorganic chemistry: Active sites in non-heme iron enzymes
    • Solomon, E. I. (2001) Geometric and electronic structure contributions to function in bioinorganic chemistry: Active sites in non-heme iron enzymes Inorg. Chem. 40, 3656-3669
    • (2001) Inorg. Chem. , vol.40 , pp. 3656-3669
    • Solomon, E.I.1
  • 32
    • 0033566802 scopus 로고    scopus 로고
    • Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions
    • Sugimoto, K., Senda, T., Aoshima, H., Masai, E., Fukuda, M., and Mitsui, Y. (1999) Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions Structure (London) 7, 953-965
    • (1999) Structure (London) , vol.7 , pp. 953-965
    • Sugimoto, K.1    Senda, T.2    Aoshima, H.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 33
    • 6344291632 scopus 로고    scopus 로고
    • Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: Site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)
    • Mendel, S., Arndt, A., and Bugg, T. D. H. (2004) Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: Site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB) Biochemistry 43, 13390-13396
    • (2004) Biochemistry , vol.43 , pp. 13390-13396
    • Mendel, S.1    Arndt, A.2    Bugg, T.D.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.