Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200.

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. Inorg Chem (2015) 0.79

Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies. Inorg Chem (2016) 0.75

Rearrangements of organic peroxides and related processes. Beilstein J Org Chem (2016) 0.75

Assessment of microcrystal quality by transmission electron microscopy for efficient serial femtosecond crystallography. Arch Biochem Biophys (2016) 0.75

Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science (2007) 3.03

Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science (1995) 2.68

Finding intermediates in the O2 activation pathways of non-heme iron oxygenases. Acc Chem Res (2007) 2.64

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat Chem Biol (2008) 2.64

The ins and outs of ring-cleaving dioxygenases. Crit Rev Biochem Mol Biol (2006) 2.36

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 (1996) 1.98

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 dioxygenases. J Biol Chem (1986) 1.86

Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J Bacteriol (2004) 1.84

X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Biochemistry (1995) 1.70

Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proc Natl Acad Sci U S A (2010) 1.57

Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates. Biochemistry (2005) 1.57

Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase. Biochemistry (2004) 1.48

EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment. J Biol Chem (1983) 1.47

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 (2002) 1.45

Mechanism of extradiol aromatic ring-cleaving dioxygenases. Curr Opin Struct Biol (2008) 1.43

Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity. J Biol Chem (1996) 1.43

Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases. J Am Chem Soc (2004) 1.39

Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure (1999) 1.27

A density functional investigation of the extradiol cleavage mechanism in non-heme iron catechol dioxygenases. J Biol Inorg Chem (2003) 1.19

Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Biochemistry (2008) 1.11

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 (2004) 1.08

Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates. Biochemistry (2011) 1.07

A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase. J Biol Inorg Chem (2010) 1.06

Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant. Biochemistry (2012) 0.97

Substrate specificity of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone 1,2-dioxygenase. Biochemistry (2011) 0.97

Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation. Biochemistry (2012) 0.94

Catalytic reaction mechanism of homogentisate dioxygenase: a hybrid DFT study. J Am Chem Soc (2005) 0.94

Characterizing the promiscuity of LigAB, a lignin catabolite degrading extradiol dioxygenase from Sphingomonas paucimobilis SYK-6. Biochemistry (2013) 0.84

Reaction mechanism of homoprotocatechuate 2,3-dioxygenase with 4-nitrocatechol: implications for the role of substrate. J Phys Chem B (2014) 0.79

Crystal structure and functional analysis of the extradiol dioxygenase LapB from a long-chain alkylphenol degradation pathway in Pseudomonas. J Biol Chem (2009) 0.79