Heather R. Williamson, Ph.D.
Affiliations: | 2006-2013 | Chemistry | California Institute of Technology, Pasadena, CA |
| 2013-2016 | Burnett School of Biomedical Sciences | University of Central Florida, Orlando, FL, United States | |
| 2016- | Chemistry | Xavier University of Louisiana, USA |
Area:
Bioinorganic chemistry, Electron-transfer chemistryGoogle:
"Heather Williamson"Mean distance: 7.31 | S | N | B | C | P |
Parents
Sign in to add mentor| Harry Barkus Gray | grad student | 2013 | Caltech | |
| (Engineering multi-step electron tunneling systems in proteins.) | ||||
| Victor L. Davidson | post-doc | 2013- | University of Central Florida | |
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Publications
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| Takematsu K, Williamson HR, Nikolovski P, et al. (2019) Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein. Acs Central Science. 5: 192-200 |
| Williamson HR, Sehanobish E, Shiller AM, et al. (2017) Roles of copper and a conserved aspartic acid in the autocatalytic hydroxylation of a specific tryptophan residue during cysteine tryptophylquinone biogenesis. Biochemistry |
| Sehanobish E, Williamson HR, Davidson VL. (2016) Roles of conserved residues of GoxA in controlling glycine oxidase activity, cooperativity, subunit composition and cysteine tryptophylquinone biosynthesis. The Journal of Biological Chemistry |
| Ma Z, Williamson HR, Davidson VL. (2016) A suicide mutation affecting proton transfers to high-valent hemes causes inactivation of MauG during catalysis. Biochemistry |
| Ma Z, Williamson HR, Davidson VL. (2016) Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent hemes. The Biochemical Journal |
| Sehanobish E, Camprillo-Brocal JC, Williamson HR, et al. (2016) Interaction of GoxA with its modifying enzyme and its subunit assembly are dependent on the extent of cysteine tryptophylquinone biosynthesis. Biochemistry |
| Ma Z, Williamson HR, Davidson VL. (2015) Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG. Proceedings of the National Academy of Sciences of the United States of America. 112: 10896-901 |
| Shin S, Feng M, Li C, et al. (2015) A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent Fe(II)/Fe(III) state and enhances charge resonance stabilization of the bis-Fe(IV) state. Biochimica Et Biophysica Acta. 1847: 709-16 |
| Williamson HR, Dow BA, Davidson VL. (2014) Mechanisms for control of biological electron transfer reactions. Bioorganic Chemistry. 57: 213-21 |
| Shin S, Choi M, Williamson HR, et al. (2014) A simple method to engineer a protein-derived redox cofactor for catalysis. Biochimica Et Biophysica Acta. 1837: 1595-601 |