Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies

scientific article published on 08 June 2016

Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies is …
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P6179Dimensions Publication ID1055093590
P356DOI10.1021/ACS.INORGCHEM.6B00148
P6366Microsoft Academic ID2418173092
P932PMC publication ID4924929
P698PubMed publication ID27275865

P50authorJohn D. LipscombQ38327124
Katlyn MeierQ58807103
P2093author name stringElena G Kovaleva
Melanie S Rogers
Eckard Münck
Emile L Bominaar
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Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200Q36021557
A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods.Q36240394
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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Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substratesQ39327808
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
Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenaseQ45165821
Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediatesQ46480177
Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coliQ46517404
Invited award contribution for ACS Award in Inorganic Chemistry. Geometric and electronic structure contributions to function in bioinorganic chemistry: active sites in non-heme iron enzymesQ48367790
EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environmentQ50169852
Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity.Q52308271
X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanismQ57943724
Spectroscopic studies of isopenicillin N synthase. A mononuclear nonheme Fe2+ oxidase with metal coordination sites for small molecules and substrateQ69361593
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P433issue12
P407language of work or nameEnglishQ1860
P304page(s)5862-5870
P577publication date2016-06-08
P1433published inInorganic ChemistryQ902828
P859sponsorReaction intermediates in the O2 activation mechanism of an extradiol dioxygenase: visualising catalytic protons and active site dynamics in crystalloQ63346673
P1476titleEnzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies
P478volume55