Hemoglobin conformation couples erythrocyte S-nitrosothiol content to O(2) gradients

It is proposed that the bond between nitric oxide (NO) and the Hb thiol Cys-β(93) (SNOHb) is favored when hemoglobin (Hb) is in the relaxed (R, oxygenated) conformation, and that deoxygenation to tense (T) state destabilizes the SNOHb bond, allowing transfer of NO from Hb to form other (vasoactive)...

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Главные авторы: Doctor, Allan, Platt, Ruth, Sheram, Mary Lynn, Eischeid, Anne, McMahon, Timothy, Maxey, Thomas, Doherty, Joseph, Axelrod, Mark, Kline, Jaclyn, Gurka, Matthew, Gow, Andrew, Gaston, Benjamin
Формат: Artigo
Язык:Inglês
Опубликовано: National Academy of Sciences 2005
Предметы:
Biological Sciences
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC556285/
https://ncbi.nlm.nih.gov/pubmed/15824313
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0407490102
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