title: Contrasting observations on buffer catalysis of guanosine amino proton exchange.
abstract: The two amino protons of 3', 5'-cyclic guanosine monophosphate are shown to differ drastically in their solvent exchange properties: One is rapidly exchanging and sensitive to buffer catalysis; the other slow and insensitive. This observation accounts for the marked contrast between stopped-flow and NMR observations on buffer catalysis of amino proton exchange in guanosine monophosphates. The amino protons of guanine compounds traverse a "fast" solvent exchange position through the process of amino rotation, which together with kinetic considerations and comparative data on adenine and cytosine compounds, supports proposals of solvent exchange mediated by events at the guanine (N-3) site, rather than the (N-7) site. Exchange does not conform to rate expressions used by different workers for amino proton exchange.
authors.affiliation: Department of Biochemistry and Biophysics, John A. Burns School of Medicine, Honolulu, HA 96822.
authors.forename: B
authors.initials: B
authors.lastname: McConnell
mesh_terms: D002021:Buffers; D002384:Catalysis; D006152:Cyclic GMP / Q000031:analogs & derivatives; D006151:Guanosine; D009682:Magnetic Resonance Spectroscopy; D011522:Protons; D012997:Solvents; D013053:Spectrophotometry
chemical_list: D002021:Buffers; D011522:Protons; D012997:Solvents; D006151:Guanosine; D006152:Cyclic GMP