Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases

scientific article published on April 2004

Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/JB.186.7.1945-1958.2004
P932PMC publication ID374394
P698PubMed publication ID15028678

P50authorLawrence P. WackettQ76490493
P2093author name stringMatthew W Vetting
John D Lipscomb
Lawrence Que
Douglas H Ohlendorf
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Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenasesQ36424496
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Gentisate 1,2-dioxygenase from Haloferax sp. D1227.Q43026034
Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8.Q43032877
Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexesQ43634839
Extradiol oxidative cleavage of catechols by ferrous and ferric complexes of 1,4,7-triazacyclononane: insight into the mechanism of the extradiol catechol dioxygenasesQ43678118
The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates.Q43798555
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.Q43915522
4-nitrocatechol as a probe of a Mn(II)-dependent extradiol-cleaving catechol dioxygenase (MndD): comparison with relevant Fe(II) and Mn(II) model complexesQ44317550
Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzymeQ44593481
Complete nucleotide sequence of the metapyrocatechase gene on the TOI plasmid of Pseudomonas putida mt-2.Q48399500
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X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanismQ57943724
Nature of the Iron–Oxygen Bond in OxyhæmoglobinQ59066076
[17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenasesQ70106014
Crystallization and Some Properties of 3,4-Dihydroxyphenylacetate 2,3-Oxygenase from Pseudomonas Ovalis*Q72632509
The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putidaQ72793143
Mutational and spectroscopic studies of the significance of the active site glutamine to metal ion specificity in superoxide dismutaseQ72990659
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P433issue7
P407language of work or nameEnglishQ1860
P921main subjectmanganeseQ731
P304page(s)1945-1958
P577publication date2004-04-01
P1433published inJournal of BacteriologyQ478419
P1476titleCrystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases
P478volume186

Reverse relations

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