The solid-state molecular structure of the S-nitroso derivative of L-cysteine ethyl ester hydrochloride.
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.
Yi
Jun
J
Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA.
Khan
Masood A
MA
Lee
Jonghyuk
J
Richter-Addo
George B
GB
D000478:Alkylation; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000031:analogs & derivatives* / Q000737:chemistry; D015394:Molecular Structure; D009569:Nitric Oxide / Q000737:chemistry; D009603:Nitroso Compounds / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry
D009603:Nitroso Compounds; C429310:S-nitrosocysteine ethyl ester; D013438:Sulfhydryl Compounds; D009569:Nitric Oxide; D003545:Cysteine