Search results for: David P. Ballou

Items from 1 to 20 out of 63 results

article

Protonation status and control mechanism of flavin–oxygen intermediates in the reaction of bacterial luciferase

Ruchanok Tinikul, Narin Lawan, Nattanon Akeratchatapan, Panu Pimviriyakul, more

The FEBS Journal > 288 > 10 > 3246 - 3260

Bacterial luciferase catalyzes a bioluminescent reaction by oxidizing long‐chain aldehydes to acids using reduced FMN and oxygen as co‐substrates. Although a flavin C4a‐peroxide anion is postulated to be the intermediate reacting with aldehyde prior to light liberation, no clear identification of the protonation status of this intermediate has been reported. Here, transient kinetics, pH variation,...

article

Characterization of a new Baeyer-Villiger monooxygenase and conversion to a solely N-or S-oxidizing enzyme by a single R292 mutation

Gianluca Catucci, Ivan Zgrablic, Francesco Lanciani, Francesca Valetti, more

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics > 2016 > 1864 > 9 > 1177-1187

Ar-BVMO is a recently discovered Baeyer-Villiger monooxygenase from the genome of Acinetobacter radioresistens S13 closely related to medically relevant ethionamide monooxygenase EtaA (prodrug activator) and capable of inactivating the imipenem antibiotic.The co-substrate preference as well as steady-state and rapid kinetics studies of the recombinant purified protein were carried out using stopped-flow...

article

Oxidative hemoglobin reactions: Applications to drug metabolism

Tatyana Spolitak, Paul F. Hollenberg, David P. Ballou

Archives of Biochemistry and Biophysics > 2016 > 600 > C > 33-46

Hb is a protein with multiple functions, acting as an O₂ transport protein, and having peroxidase and oxidase activities with xenobiotics that lead to substrate radicals. However, there is a lack of evidence for intermediates involved in these reactions of Hb with redox-active compounds, including those with xenobiotics such as drugs, chemical carcinogens, and sulfides. In particular, questions exist...

article

Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine P-Synthase

Sebastian Carballal, Carmen Gherasim, Pramod K. Yadav, Ernesto Cuevasanta, more

Free Radical Biology and Medicine > 2015 > 87 > S1 > S123

article

Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD

Tatyana Spolitak, David P. Ballou

Archives of Biochemistry and Biophysics > 2015 > 573 > Complete > 111-119

We provide the first experimental evidence for intermediates being involved in catalysis by RebD in generating the chromopyrrolic acid (CPA) scaffold of rebeccamycin. In the presence of its substrates (indole pyruvate imine – IPAI – and H ₂ O ₂ both produced by the flavoprotein oxidase RebO that oxidizes tryptophan), RebD reacts as a peroxidase forming two IPAI radicals that recombine...

article

The Heme in Human Cystathionine ?-Synthase: Kinetics of Reduction and Reoxidation

Sebastián Carballa, Ernesto Cuevasanta, Inés Marmisolle, Omer Kabil, more

Free Radical Biology and Medicine > 2012 > 53 > Supplement 2 > S146

article

Studies with bilirubin and toxicological implications of uncoupling

Francesco De Matteis, David P. Ballou, Minor J. Coon, Ronald W. Estabrook, more

Biochemical Pharmacology > 2012 > 84 > 3 > 374-382

The NADPH-dependent consumption of O ₂ by cytochrome P450 BM3 was stimulated by either laurate or perfluorolaurate, but the NADPH/O ₂ molar consumption ratios were approximately 1 and 2, respectively, indicating that perfluorolaurate does not become oxygenated by BM3 and oxygen undergoes full reduction to water. The nature of this catalytic cycle uncoupled to hydroxylation was explored...

article

Reactivity of Thioredoxin as a Protein Thiol-Disulfide Oxidoreductase

Zhiyong Cheng, Jinfeng Zhang, David P. Ballou, Charles H. Williams

Chemical Reviews > 2011 > 111 > 9 > 5768 - 5783

article

Investigations of the Catalytic Mechanism of Thioredoxin Glutathione Reductase from Schistosoma mansoni

Hsin-Hung Huang, Latasha Day, Cynthia L. Cass, David P. Ballou, more

Biochemistry > 2011 > 50 > 26 > 5870 - 5882

article

Elucidating the Role of the Proximal Cysteine Hydrogen-Bonding Network in Ferric Cytochrome P450cam and Corresponding Mutants Using Magnetic Circular Dichroism Spectroscopy

Mary Grace I. Galinato, Tatyana Spolitak, David P. Ballou, Nicolai Lehnert

Biochemistry > 2011 > 50 > 6 > 1053 - 1069

article

Pre-Steady-State Kinetic Analysis of Enzyme-Monitored Turnover during Cystathionine β-Synthase-Catalyzed H ₂ S Generation

Sangita Singh, David P. Ballou, Ruma Banerjee

Biochemistry > 2011 > 50 > 3 > 419 - 425

article

Reduction Kinetics of a Flavin Oxidoreductase LuxG from Photobacterium leiognathi (TH1): Half-Sites Reactivity

Sarayut Nijvipakul, David P. Ballou, Pimchai Chaiyen

Biochemistry > 2010 > 49 > 43 > 9241 - 9248

article

Studies on the Mechanism of p- Hydroxyphenylacetate 3-Hydroxylase from Pseudomonas aeruginosa : A System Composed of a Small Flavin Reductase and a Large Flavin-Dependent Oxygenase

Sumita Chakraborty, Mariliz Ortiz-Maldonado, Barrie Entsch, David P. Ballou

Biochemistry > 2010 > 49 > 2 > 372 - 385

article

Spectroscopic studies of the oxidation of ferric CYP153A6 by peracids: Insights into P450 higher oxidation states

Tatyana Spolitak, Enrico G. Funhoff, David P. Ballou

Archives of Biochemistry and Biophysics > 2010 > 493 > 2 > 184-191

Our previous rapid-scanning stopped-flow studies of the reaction of substrate-free cytochrome P450cam with peracids [T. Spolitak, J.H. Dawson, D.P. Ballou, J. Biol. Chem. 280 (2005) 20300–20309; J. Inorg. Biochem. 100 (2006) 2034–2044; J. Biol. Inorg. Chem. 13 (2008) 599–611] spectrally characterized compound I (ferryl iron plus a porphyrin π-cation radical (Fe ^IV O/Por ⁺ )), Cpd ES,...

article

Functional Role for the Conformationally Mobile Phenylalanine 223 in the Reaction of Methylenetetrahydrofolate Reductase from Escherichia coli

Moon N. Lee, Desire Takawira, Andriana P. Nikolova, David P. Ballou, more

Biochemistry > 2009 > 48 > 32 > 7673 - 7685

article

Distal end of 105–125 loop – A putative reductase binding domain of phthalate dioxygenase

Michael Tarasev, Sailaja Pullela, David P. Ballou

Archives of Biochemistry and Biophysics > 2009 > 487 > 1 > 10-18

The phthalate dioxygenase system consists of the dioxygenase, PDO, which contains a Rieske [2Fe–2S] center and a Fe(II)-mononuclear center, and the reductase, PDR. Involvement of the distal end of the 105–125 loop of PDO in its interaction with PDR was tested by substituting charged residues in the loop with alanines and by replacing the conserved tryptophan-94. Compared to wild-type PDO, all variants...

article

Function of Glu-469′ in the Acid−Base Catalysis of Thioredoxin Reductase from Drosophila melanogaster ^†

Hsin-Hung Huang, L. David Arscott, David P. Ballou, Charles H. Williams

Biochemistry > 2008 > 47 > 48 > 12769 - 12776

article

γ-Glutamyl Hydrolase: Kinetic Characterization of Isopeptide Hydrolysis Using Fluorogenic Substrates ^†

Jessica P. Alexander, Thomas J. Ryan, David P. Ballou, James K. Coward

Biochemistry > 2008 > 47 > 4 > 1228 - 1239

article

Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants

Tatyana Spolitak, John H. Dawson, David P. Ballou

JBIC Journal of Biological Inorganic Chemistry > 2008 > 13 > 4 > 599-611

Our previous rapid-scanning stopped-flow studies of the reaction of substrate-free cytochrome P450cam with peracids [Spolitak et al. (2005) J Biol Chem 280:20300–20309; (2006) J Inorg Biochem 100:2034–2044] spectrally characterized compound I [ferryl iron plus a porphyrin π-cation radical (Fe^IV=O/Por^·+)], as well as Cpd ES (Fe^IV=O/Tyr·). In the present studies, we report how the substitutions in Y75F,...

article

Similar enzymes, different structures: Phthalate dioxygenase is an α3α3 stacked hexamer, not an α3β3 trimer like “normal” Rieske oxygenases

Michael Tarasev, Catherine S. Kaddis, Sheng Yin, Joseph A. Loo, more

Archives of Biochemistry and Biophysics > 2007 > 466 > 1 > 31-39

Phthalate dioxygenase (PDO) is a member of a class of bacterial oxygenases that contain both Rieske [2Fe–2S] and Fe(II) mononuclear centers. Recent crystal structures of several Rieske dioxygenases showed that they exist as α ₃ β ₃ multimers with subunits arranged head-to-tail in α and β stacked planar rings. The structure of PDO, which consists of only α-subunits, remains to be solved...

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Search results for: David P. Ballou

Protonation status and control mechanism of flavin–oxygen intermediates in the reaction of bacterial luciferase

Characterization of a new Baeyer-Villiger monooxygenase and conversion to a solely N-or S-oxidizing enzyme by a single R292 mutation

Oxidative hemoglobin reactions: Applications to drug metabolism

Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine P-Synthase

Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD

The Heme in Human Cystathionine ?-Synthase: Kinetics of Reduction and Reoxidation

Studies with bilirubin and toxicological implications of uncoupling

Reactivity of Thioredoxin as a Protein Thiol-Disulfide Oxidoreductase

Investigations of the Catalytic Mechanism of Thioredoxin Glutathione Reductase from Schistosoma mansoni

Elucidating the Role of the Proximal Cysteine Hydrogen-Bonding Network in Ferric Cytochrome P450cam and Corresponding Mutants Using Magnetic Circular Dichroism Spectroscopy

Pre-Steady-State Kinetic Analysis of Enzyme-Monitored Turnover during Cystathionine β-Synthase-Catalyzed H ₂ S Generation

Reduction Kinetics of a Flavin Oxidoreductase LuxG from Photobacterium leiognathi (TH1): Half-Sites Reactivity

Studies on the Mechanism of p- Hydroxyphenylacetate 3-Hydroxylase from Pseudomonas aeruginosa : A System Composed of a Small Flavin Reductase and a Large Flavin-Dependent Oxygenase

Spectroscopic studies of the oxidation of ferric CYP153A6 by peracids: Insights into P450 higher oxidation states

Functional Role for the Conformationally Mobile Phenylalanine 223 in the Reaction of Methylenetetrahydrofolate Reductase from Escherichia coli

Distal end of 105–125 loop – A putative reductase binding domain of phthalate dioxygenase

Function of Glu-469′ in the Acid−Base Catalysis of Thioredoxin Reductase from Drosophila melanogaster ^†

γ-Glutamyl Hydrolase: Kinetic Characterization of Isopeptide Hydrolysis Using Fluorogenic Substrates ^†

Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants

Similar enzymes, different structures: Phthalate dioxygenase is an α3α3 stacked hexamer, not an α3β3 trimer like “normal” Rieske oxygenases

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