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Noncovalent interactions dominate dynamic heme distortion in cytochrome P450 4B1

Cytochrome P450 4B1 (4B1) functions in both xenobiotic and endobiotic metabolism. An ester linkage between Glu-310 in 4B1 and the 5-methyl group of heme facilitates preferential hydroxylation of terminal (ω) methyl groups of hydrocarbons (HCs) and fatty acids compared with ω–1 sites bearing weaker C...

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Библиографические подробности
Опубликовано в: :J Biol Chem
Главные авторы: Jennings, Gareth K., Hsu, Mei-Hui, Shock, Lisa S., Johnson, Eric F., Hackett, John C
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2018
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC6065186/
https://ncbi.nlm.nih.gov/pubmed/29858244
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.004044
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