Zobrazeno 1 - 10
of 344
pro vyhledávání: '"Thomas L Poulos"'
Autor:
Ariel Lewis-Ballester, Khoa N. Pham, Dipanwita Batabyal, Shay Karkashon, Jeffrey B. Bonanno, Thomas L. Poulos, Syun-Ru Yeh
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
Human indoleamine 2,3-dioxygenase 1 (hIDO1) is an immunotherapeutic target for cancer therapy. Here, the authors present the substrate-, inhibitor- and effector-bound hIDO1 crystal structures, which give insights into the mechanism and reveal a secon
Externí odkaz:
https://doaj.org/article/f8b733a4df2546f48fc72aa65deeac3d
Autor:
Xinke Wang, Weihong Wang, Lisa M. Wingen, Véronique Perraud, Michael J. Ezell, Jessica Gable, Thomas L. Poulos, Barbara J. Finlayson-Pitts
Publikováno v:
Science advances, vol 9, iss 9
While nitro and amino alkenes are common in pharmaceuticals, pesticides, and munitions, their environmental fates are not well known. Ozone is a ubiquitous atmospheric oxidant for alkenes, but the synergistic effects of nitrogen-containing groups on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6b7554cf14acf726ef470b64f3694ef
https://escholarship.org/uc/item/6kb150t2
https://escholarship.org/uc/item/6kb150t2
Autor:
Thomas L. Poulos, Alec H. Follmer
Publikováno v:
Acc Chem Res
This Account summarizes recent findings centered on the role that redox partner binding, allostery, and conformational dynamics plays in cytochrome P450 proton coupled electron transfer. P450s are one of Nature’s largest enzyme families and it is n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18b88a405e7c306ebeaf3406af945ef5
https://pubmed.ncbi.nlm.nih.gov/34965086
https://pubmed.ncbi.nlm.nih.gov/34965086
Autor:
Simon P. Skinner, Emanuele Paci, Thomas L. Poulos, Jeanine J. Houwing-Duistermaat, Alec H. Follmer, Marcellus Ubbink
Publikováno v:
Biochemistry, 60(39), 2932-2942. American Chemical Society (ACS)
Biochemistry
Biochemistry
Cytochrome P450cam (CYP101A1) catalyzes the region- and stereo-specific 5-exo-hydroxylation of camphor via a multistep catalytic cycle that involves two-electron transfer steps, with an absolute requirement that the second electron be donated by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::603eeb8a232e1e0288e6c42d3ac534ae
https://doi.org/10.1021/acs.biochem.1c00406
https://doi.org/10.1021/acs.biochem.1c00406
Publikováno v:
Journal of Inorganic Biochemistry. 244:112212
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f186b86bccae03da93853bcf78c0cb4f
https://doi.org/10.1016/j.jinorgbio.2023.112212
https://doi.org/10.1016/j.jinorgbio.2023.112212
Publikováno v:
Biochemistry
Cytochrome P450s are among nature’s most powerful catalysts. Their ability to activate molecular dioxygen to form high-valent ferryl intermediates (Compounds I and II) enables a wide array of chemistries ranging from simple epoxidations to more com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d47162273475f36ab9ba741e7150400
https://doi.org/10.1021/acs.biochem.0c00329
https://doi.org/10.1021/acs.biochem.0c00329
Publikováno v:
Biochemistry
The bacterial cytochrome P450cam catalyzes the oxidation of camphor to 5-exo-hydroxycamphor as the first step in the oxidative assimilation of camphor as a carbon/energy source. CYP101D1 is another bacterial P450 that catalyzes the same reaction. A t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c43d7502cc53b3d466820e2deacc2ae7
https://doi.org/10.1021/acs.biochem.0c00366
https://doi.org/10.1021/acs.biochem.0c00366
Publikováno v:
ACS omega. 7(22)
A characteristic feature of cytochromes P450* is that the complex formed between the ferrous heme iron and carbon monoxide generates an intense absorption band at 450 nm. This unique feature of P450s is due to the proximal thiolate Cys ligand coordin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ba816bbb34e49d3625236292ac605e4
https://pubmed.ncbi.nlm.nih.gov/35694512
https://pubmed.ncbi.nlm.nih.gov/35694512
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 27(2)
Three well-characterized heme peroxidases (cytochrome c peroxidase = CCP, ascorbate peroxidase = APX, and Leishmania major peroxidase = LMP) all have a Trp residue tucked under the heme stacked against the proximal His heme ligand. The reaction of pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78cea24cd67daa9870b4056786460c04
https://pubmed.ncbi.nlm.nih.gov/35064363
https://pubmed.ncbi.nlm.nih.gov/35064363
Autor:
Jose A. Amaya, David C. Lamb, Steven L. Kelly, Patrick Caffrey, Vidhi C. Murarka, Thomas L. Poulos
Publikováno v:
The Journal of biological chemistry, vol 298, iss 4
AmphL is a cytochrome P450 enzyme that catalyzes the C8 oxidation of 8-deoxyamphotericin B to the polyene macrolide antibiotic, amphotericin B. To understand this substrate selectivity, we solved the crystal structure of AmphL to a resolution of 2.0
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59aaeca359e1e3fcd011ba0fce979c5f
https://doi.org/10.1016/j.jbc.2022.101746
https://doi.org/10.1016/j.jbc.2022.101746