Search Results - "Pierce, Brad S"
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Cyanide replaces substrate in obligate-ordered addition of nitric oxide to the non-heme mononuclear iron AvMDO active site
Published in Journal of biological inorganic chemistry (01-04-2023)“…Thiol dioxygenases are a subset of non-heme mononuclear iron oxygenases that catalyze the O 2 -dependent oxidation of thiol-bearing substrates to yield…”
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Aminoquinoline-Based Tridentate ( NNN )-Copper Catalyst for C-N Bond-Forming Reactions from Aniline and Diazo Compounds
Published in Molecules (Basel, Switzerland) (01-02-2024)“…A new tridentate Cu complex based on ( )-1-(pyridin-2-yl)- -(quinolin-8-yl)methanimine (PQM) was generated and characterized to support the activation of diazo…”
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3
Spectroscopic and Computational Characterization of Substrate-Bound Mouse Cysteine Dioxygenase: Nature of the Ferrous and Ferric Cysteine Adducts and Mechanistic Implications
Published in Biochemistry (Easton) (27-07-2010)“…Cysteine dioxygenase (CDO) is a mononuclear non-heme Fe-dependent dioxygenase that catalyzes the initial step of oxidative cysteine catabolism. Its active site…”
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4
Metallodithiolates as Ligands to Dinitrosyl Iron Complexes: Toward the Understanding of Structures, Equilibria, and Spin Coupling
Published in Inorganic chemistry (02-09-2014)“…Metallodithiolate ligands are used to design heterobimetallic complexes by adduct formation through S-based reactivity. Such adducts of dinitrosyl iron were…”
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5
Free ferrous ions sustain activity of mammalian stearoyl-CoA desaturase-1
Published in The Journal of biological chemistry (01-07-2023)“…Mammalian stearoyl-CoA desaturase-1 (SCD1) introduces a double-bond to a saturated long-chain fatty acid in a reaction catalyzed by a diiron center. The diiron…”
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6
Abiological catalysis by myoglobin mutant with a genetically incorporated unnatural amino acid
Published in Biochemical journal (14-05-2021)“…To inculcate biocatalytic activity in the oxygen-storage protein myoglobin (Mb), a genetically engineered myoglobin mutant H64DOPA (DOPA =…”
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7
1,2-Disubstituted Benzimidazoles by the Iron Catalyzed Cross-Dehydrogenative Coupling of Isomeric o‑Phenylenediamine Substrates
Published in Journal of organic chemistry (21-02-2020)“…Benzimidazoles are common in nature, medicines, and materials. Numerous strategies for preparing 2-arylbenzimidazoles exist. In this work, 1,2-disubstituted…”
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Outer-Sphere Tyrosine 159 within the 3‑Mercaptopropionic Acid Dioxygenase S‑H‑Y Motif Gates Substrate-Coordination Denticity at the Non-Heme Iron Active Site
Published in Biochemistry (Easton) (24-12-2019)“…Thiol dioxygenases are non-heme mononuclear iron enzymes that catalyze the O2-dependent oxidation of free thiols (-SH) to produce the corresponding sulfinic…”
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9
Isoindolinone Synthesis: Selective Dioxane-Mediated Aerobic Oxidation of Isoindolines
Published in Journal of organic chemistry (18-01-2019)“…N-Alkyl and N-aryl-isoindolinones were prepared by a dioxane-mediated oxidation of isoindoline precursors. The transformation exhibits unique chemoselectivity…”
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Low-Spin Cyanide Complexes of 3-Mercaptopropionic Acid Dioxygenase (MDO) Reveal the Impact of Outer-Sphere SHY-Motif Residues
Published in Inorganic chemistry (20-12-2021)“…3-Mercaptopropionic acid ( ) dioxygenase (MDO) is a non-heme Fe(II)/O -dependent oxygenase that catalyzes the oxidation of thiol-substrates to yield the…”
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Recombinant expression, purification, and characterization of ThmD, the oxidoreductase component of tetrahydrofuran monooxygenase
Published in Archives of biochemistry and biophysics (15-04-2010)“…Tetrahydrofuran monooxygenase (Thm) catalyzes the NADH-and oxygen-dependent hydroxylation of tetrahydrofuran to 2-hydroxytetrahydrofuran. Thm is composed of a…”
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12
Catalytic hydrogen atom transfer from hydrosilanes to vinylarenes for hydrosilylation and polymerization
Published in Nature catalysis (01-02-2019)Get full text
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13
Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase
Published in Archives of biochemistry and biophysics (01-01-2015)“…[Display omitted] •Cysteine dioxygenase (CDO) catalyzes formation of several sulfinic acid products.•Substrate-specificity (V/K) for CDO can be measured over…”
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14
Cooperative redox and spin activity from three redox congeners of sulfur-bridged iron nitrosyl and nickel dithiolene complexes
Published in Proceedings of the National Academy of Sciences - PNAS (21-06-2022)“…The synthesis of sulfur-bridged Fe-Ni heterobimetallics was inspired by Nature's strategies to "trick" abundant first row transition metals into enabling…”
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15
Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center
Published in The Journal of biological chemistry (01-01-2021)“…Thiol dioxygenases are a subset of nonheme iron oxygenases that catalyze the formation of sulfinic acids from sulfhydryl-containing substrates and dioxygen…”
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Single Turnover of Substrate-Bound Ferric Cysteine Dioxygenase with Superoxide Anion: Enzymatic Reactivation, Product Formation, and a Transient Intermediate
Published in Biochemistry (Easton) (29-11-2011)“…Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the O2-dependent oxidation of l-cysteine (Cys) to produce cysteine sulfinic…”
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17
Magnetic coupling between Fe(NO) spin probe ligands through diamagnetic NiII, PdII and PtII tetrathiolate bridges
Published in Chemical science (Cambridge) (14-08-2023)“…Reaction of the nitrosylated-iron metallodithiolate ligand, paramagnetic (NO)Fe(N2S2), with [M(CH3CN)n][BF4]2 salts (M = NiII, PdII, and PtII; n = 4 or 6)…”
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The “Gln-Type” Thiol Dioxygenase from Azotobacter vinelandii Is a 3‑Mercaptopropionic Acid Dioxygenase
Published in Biochemistry (Easton) (29-12-2015)“…Cysteine dioxygenase (CDO) is a non-heme iron enzyme that catalyzes the O2-dependent oxidation of l-cysteine to produce cysteinesulfinic acid. Bacterial CDOs…”
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Correction: Magnetic coupling between Fe(NO) spin probe ligands through diamagnetic NiII, PdII and PtII tetrathiolate bridges
Published in Chemical science (Cambridge) (04-10-2023)“…Correction for ‘Magnetic coupling between Fe(NO) spin probe ligands through diamagnetic NiII, PdII and PtII tetrathiolate bridges’ by Manuel Quiroz et al.,…”
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Mechanistic Implications for the Formation of the Diiron Cluster in Ribonucleotide Reductase Provided by Quantitative EPR Spectroscopy
Published in Journal of the American Chemical Society (23-07-2003)“…The small subunit of Escherichia coli ribonucleotide reductase (R2) is a homodimeric (ββ) protein, in which each β-peptide contains a diiron cluster composed…”
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