Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10835217 | Nitric Oxide | 2005 | 6 Pages |
Abstract
Nitrosation of protein sulfhydryl groups to form thionitrites (S-nitrosothiols) has been reported to be important in the biochemistry of nitric oxide. Such S-nitrosation of protein thiol residues has been shown to alter the function of some proteins. In this brief communication, we report the X-ray crystal structure of S-nitroso-l-cysteine ethyl ester hydrochloride. Two rotamers with respect to the NCCS moiety are present in the crystal: the major rotamer is in the gauche+ conformation, and the minor rotamer is in the rare anti (trans, antiperiplanar) conformation for a cysteinyl compound. Importantly, the CSNO groups for both rotamers are in the syn (cis, synperiplanar) form. To the best of our knowledge, this is the first reported high-resolution solid-state structure of an S-nitroso derivative of a cysteine or cysteinyl-containing compound.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Jun Yi, Masood A. Khan, Jonghyuk Lee, George B. Richter-Addo,