Cytochrome c-mediated formation of S-nitrosothiol in cells. Biochem J 2012 Feb 15;442(1):191-7
Date
11/11/2011Pubmed ID
22070099Pubmed Central ID
PMC3943432DOI
10.1042/BJ20111294Scopus ID
2-s2.0-84856239300 (requires institutional sign-in at Scopus site) 38 CitationsAbstract
S-nitrosothiols are products of nitric oxide (NO) metabolism that have been implicated in a plethora of signalling processes. However, mechanisms of S-nitrosothiol formation in biological systems are uncertain, and no efficient protein-mediated process has been identified. Recently, we observed that ferric cytochrome c can promote S-nitrosoglutathione formation from NO and glutathione by acting as an electron acceptor under anaerobic conditions. In the present study, we show that this mechanism is also robust under oxygenated conditions, that cytochrome c can promote protein S-nitrosation via a transnitrosation reaction and that cell lysate depleted of cytochrome c exhibits a lower capacity to synthesize S-nitrosothiols. Importantly, we also demonstrate that this mechanism is functional in living cells. Lower S-nitrosothiol synthesis activity, from donor and nitric oxide synthase-generated NO, was found in cytochrome c-deficient mouse embryonic cells as compared with wild-type controls. Taken together, these data point to cytochrome c as a biological mediator of protein S-nitrosation in cells. This is the most efficient and concerted mechanism of S-nitrosothiol formation reported so far.
Author List
Broniowska KA, Keszler A, Basu S, Kim-Shapiro DB, Hogg NAuthors
Neil Hogg PhD Sr Associate Dean, Professor in the Biophysics department at Medical College of WisconsinAgnes Keszler PhD Research Scientist I in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AerobiosisAnaerobiosis
Animals
Antimycin A
Cells, Cultured
Cytochromes c
Embryo, Mammalian
Glutathione
Mice
Nitric Oxide
Nitric Oxide Synthase Type II
S-Nitrosothiols
