Search Results - "Pierce, Brad S"

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  1. 1

    Cyanide replaces substrate in obligate-ordered addition of nitric oxide to the non-heme mononuclear iron AvMDO active site by York, Nicholas J., Lockart, Molly M., Schmittou, Allison N., Pierce, Brad S.

    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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  2. 2

    Aminoquinoline-Based Tridentate ( NNN )-Copper Catalyst for C-N Bond-Forming Reactions from Aniline and Diazo Compounds by Teimouri, Mohsen, Raju, Selvam, Acheampong, Edward, Schmittou, Allison N, Donnadieu, Bruno, Wipf, David O, Pierce, Brad S, Stokes, Sean L, Emerson, Joseph P

    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. 3

    Spectroscopic and Computational Characterization of Substrate-Bound Mouse Cysteine Dioxygenase: Nature of the Ferrous and Ferric Cysteine Adducts and Mechanistic Implications by Gardner, Jessica D, Pierce, Brad S, Fox, Brian G, Brunold, Thomas C

    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. 4

    Metallodithiolates as Ligands to Dinitrosyl Iron Complexes: Toward the Understanding of Structures, Equilibria, and Spin Coupling by Pinder, Tiffany A, Montalvo, Steven K, Hsieh, Chung-Hung, Lunsford, Allen M, Bethel, Ryan D, Pierce, Brad S, Darensbourg, Marcetta Y

    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. 5

    Free ferrous ions sustain activity of mammalian stearoyl-CoA desaturase-1 by Shen, Jiemin, Wu, Gang, Pierce, Brad S., Tsai, Ah-Lim, Zhou, Ming

    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. 6

    Abiological catalysis by myoglobin mutant with a genetically incorporated unnatural amino acid by Chand, Subhash, Ray, Sriparna, Yadav, Poonam, Samanta, Susruta, Pierce, Brad S, Perera, Roshan

    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. 7

    1,2-Disubstituted Benzimidazoles by the Iron Catalyzed Cross-Dehydrogenative Coupling of Isomeric o‑Phenylenediamine Substrates by Thapa, Pawan, Palacios, Philip M, Tran, Tam, Pierce, Brad S, Foss, Frank W

    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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  8. 8

    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 by Sardar, Sinjinee, Weitz, Andrew, Hendrich, Michael P, Pierce, Brad S

    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. 9

    Isoindolinone Synthesis: Selective Dioxane-Mediated Aerobic Oxidation of Isoindolines by Thapa, Pawan, Corral, Esai, Sardar, Sinjinee, Pierce, Brad S, Foss, Frank W

    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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  10. 10

    Low-Spin Cyanide Complexes of 3-Mercaptopropionic Acid Dioxygenase (MDO) Reveal the Impact of Outer-Sphere SHY-Motif Residues by York, Nicholas J, Lockart, Molly M, Pierce, Brad S

    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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  11. 11

    Recombinant expression, purification, and characterization of ThmD, the oxidoreductase component of tetrahydrofuran monooxygenase by Oppenheimer, Michelle, Pierce, Brad S., Crawford, Joshua A., Ray, Keith, Helm, Richard F., Sobrado, Pablo

    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. 12
  13. 13

    Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase by Li, Wei, Pierce, Brad S.

    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. 14

    Cooperative redox and spin activity from three redox congeners of sulfur-bridged iron nitrosyl and nickel dithiolene complexes by Quiroz, Manuel, Lockart, Molly M, Saber, Mohamed R, Vali, Shaik Waseem, Elrod, Lindy C, Pierce, Brad S, Hall, Michael B, Darensbourg, Marcetta Y

    “…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. 15

    Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center by York, Nicholas J., Lockart, Molly M., Sardar, Sinjinee, Khadka, Nimesh, Shi, Wuxian, Stenkamp, Ronald E., Zhang, Jianye, Kiser, Philip D., Pierce, Brad S.

    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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  16. 16

    Single Turnover of Substrate-Bound Ferric Cysteine Dioxygenase with Superoxide Anion: Enzymatic Reactivation, Product Formation, and a Transient Intermediate by Crawford, Joshua A, Li, Wei, Pierce, Brad S

    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. 17

    Magnetic coupling between Fe(NO) spin probe ligands through diamagnetic NiII, PdII and PtII tetrathiolate bridges by Quiroz, Manuel, Lockart, Molly M, Xue, Shan, Jones, Dakota, Guo, Yisong, Pierce, Brad S, Dunbar, Kim R, Hall, Michael B, Darensbourg, Marcetta Y

    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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  18. 18

    The “Gln-Type” Thiol Dioxygenase from Azotobacter vinelandii Is a 3‑Mercaptopropionic Acid Dioxygenase by Pierce, Brad S, Subedi, Bishnu P, Sardar, Sinjinee, Crowell, Joshua K

    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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  19. 19

    Correction: Magnetic coupling between Fe(NO) spin probe ligands through diamagnetic NiII, PdII and PtII tetrathiolate bridges by Quiroz, Manuel, Lockart, Molly M, Xue, Shan, Jones, Dakota, Martinez, Zachary, Guo, Yisong, Pierce, Brad S, Dunbar, Kim R, Hall, Michael B, Darensbourg, Marcetta Y

    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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  20. 20

    Mechanistic Implications for the Formation of the Diiron Cluster in Ribonucleotide Reductase Provided by Quantitative EPR Spectroscopy by Pierce, Brad S, Elgren, Timothy E, Hendrich, Michael P

    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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