Výsledky vyhledávání - "Allison M. Colthart"

NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450

Autor: Drew R. Teitz, Yihao Zhuang, Maria-Eirini Pandelia, Nathan R. Wong, Jeffrey Futcher, Thomas C. Pochapsky, Allison M. Colthart

Publikováno v: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866:126-133

The existence of a substrate-sensitive equilibrium between high spin (S=5/2) and low spin (S=1/2) ferric iron is a well-established phenomenon in the cytochrome P450 (CYP) superfamily, although its origins are still a subject of discussion. A series

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e75b2708a430c6f5b956d6f6c16675ff
https://doi.org/10.1016/j.bbapap.2017.04.003

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A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild

Autor: Yihao Zhuang, Alexander E. Ferrazzoli, Nathan R. Wong, Jeffrey Futcher, Jeffrey M. Matthews, Thomas C. Pochapsky, Deani L. Cooper, Xinyue Liu, Hannah Lloyd, Theodore M. Pochapsky, Phillix Esquea, Allison M. Colthart

Publikováno v: Journal of inorganic biochemistry. 188

A strategy for elucidating sequence determinants of function in the class of cytochrome P450 (CYP) enzymes that catalyze the first steps of terpene metabolism in wild microbiomes is described. Wild organisms that can use camphor, terpineol, pinene an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0515148a68287e71e1391adf00ee2a9b
https://pubmed.ncbi.nlm.nih.gov/30170307

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Substrate recognition by two different P450s: Evidence for conserved roles in a common fold

Autor: Drew Tietz, Allison M. Colthart, Susan Sondej Pochapsky, Thomas C. Pochapsky

Publikováno v: Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)

Cytochrome P450 monooxygenases CYP101A1 and MycG catalyze regio- and stereospecific oxidations of their respective substrates, d-camphor and mycinamicin IV. Despite the low sequence homology between the two enzymes (29% identity) and differences in s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9aa713bfe5df12f67fab8fdc7a90e040
https://pubmed.ncbi.nlm.nih.gov/29051575

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Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance

Autor: Drew Tietz, Marina Dang, Allison M. Colthart, Yuhua Ni, Thomas C. Pochapsky, Jessica L. Friedman

Publikováno v: Scientific Reports

Cytochrome P450 monooxygenases typically catalyze the insertion of one atom of oxygen from O2 into unactivated carbon-hydrogen and carbon-carbon bonds, with concomitant reduction of the other oxygen atom to H2O by NAD(P)H. Comparison of the average s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::839cce2feabb9e621e2d5d3677cf56c4
http://europepmc.org/articles/PMC4766564

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Enabling the Synthesis of Perfluoroalkyl Bicyclobutanes via 1,3 γ-Silyl Elimination

Autor: Leon J. Tilley, Allison M. Colthart, Lily N. E. Dubois, Katherine R. Whitaker, Julie L. Radziewicz, Brad D. Constant, Sean R. Corning, Christopher B. Kelly, Jacqueline T. Genovese, Ellen M. Sletten

Publikováno v: Organic Letters. 13:1646-1649

Two new bicyclobutanes were prepared from cyclobutyl systems by a novel, solvolytic, carbocation-based methodology. An electron-withdrawing perfluoroalkyl group at the incipient cationic center enhances neighboring-group participation of the γ-silyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d830e4dda2abd6c2f9218c964fb7c234
https://doi.org/10.1021/ol200121f

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