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Michael T Wilson

Showing results (91-100 of 113) with videos related to

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Journal of the American Chemical Society|January 15, 2004
Protein-template-driven formation of polynuclear iron speciesSimon A Malone, Allison Lewin, Mehmet A Kilic, et al.
The Journal of Biological Chemistry|June 19, 2014
Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobinMichael Brad Strader, Wayne A Hicks, Tigist Kassa, et al.
The Biochemical Journal|July 30, 2016
Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute designGary G A Silkstone, Rebecca S Silkstone, Michael T Wilson, et al.
Biochemistry|October 31, 2017
Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic ActivityOliver M Deacon, Andreas Ioannis Karsisiotis, Tadeo Moreno-Chicano, et al.
Angewandte Chemie (International Ed. in English)|January 22, 2021
Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H<sub>2</sub> O<sub>2</sub> but Slowly with O<sub>2</sub>Jacob Pullin, Michael T Wilson, Martin Clémancey, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 20, 2019
Reaction of O<sub>2</sub> with a diiron protein generates a mixed-valent Fe<sup>2+</sup>/Fe<sup>3+</sup> center and peroxideJustin M Bradley, Dimitri A Svistunenko, Jacob Pullin, et al.
Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)|March 26, 2024
Iron Oxidation in <i>Escherichia coli</i> Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H<sub>2</sub>O<sub>2</sub> but Slowly with O<sub>2</sub>Jacob Pullin, Michael T Wilson, Martin Clémancey, et al.
Chemical Science|May 10, 2024
The circularly permuted globin domain of androglobin exhibits atypical heme stabilization and nitric oxide interactionBrandon J Reeder, Giuseppe Deganutti, John Ukeri, et al.
Frontiers in Plant Science|December 17, 2020
A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and NitriteIrene Villar, Estíbaliz Larrainzar, Lisa Milazzo, et al.
Frontiers in Plant Science|February 11, 2021
Corrigendum: A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and NitriteIrene Villar, Estíbaliz Larrainzar, Lisa Milazzo, et al.
Pageof 12

Showing results (91-100 of 113) with videos related to

Sort By:
Pageof 12
Journal of the American Chemical Society|January 15, 2004
Protein-template-driven formation of polynuclear iron speciesSimon A Malone, Allison Lewin, Mehmet A Kilic, et al.
The Journal of Biological Chemistry|June 19, 2014
Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobinMichael Brad Strader, Wayne A Hicks, Tigist Kassa, et al.
The Biochemical Journal|July 30, 2016
Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute designGary G A Silkstone, Rebecca S Silkstone, Michael T Wilson, et al.
Biochemistry|October 31, 2017
Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic ActivityOliver M Deacon, Andreas Ioannis Karsisiotis, Tadeo Moreno-Chicano, et al.
Angewandte Chemie (International Ed. in English)|January 22, 2021
Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H<sub>2</sub> O<sub>2</sub> but Slowly with O<sub>2</sub>Jacob Pullin, Michael T Wilson, Martin Clémancey, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 20, 2019
Reaction of O<sub>2</sub> with a diiron protein generates a mixed-valent Fe<sup>2+</sup>/Fe<sup>3+</sup> center and peroxideJustin M Bradley, Dimitri A Svistunenko, Jacob Pullin, et al.
Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)|March 26, 2024
Iron Oxidation in <i>Escherichia coli</i> Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H<sub>2</sub>O<sub>2</sub> but Slowly with O<sub>2</sub>Jacob Pullin, Michael T Wilson, Martin Clémancey, et al.
Chemical Science|May 10, 2024
The circularly permuted globin domain of androglobin exhibits atypical heme stabilization and nitric oxide interactionBrandon J Reeder, Giuseppe Deganutti, John Ukeri, et al.
Frontiers in Plant Science|December 17, 2020
A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and NitriteIrene Villar, Estíbaliz Larrainzar, Lisa Milazzo, et al.
Frontiers in Plant Science|February 11, 2021
Corrigendum: A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and NitriteIrene Villar, Estíbaliz Larrainzar, Lisa Milazzo, et al.
Pageof 12