화학공학소재연구정보센터
Inorganic Chemistry, Vol.35, No.5, 1121-1125, 1996
Evaluation of Solvent Accessibility to the (Fe4S4) Binding Pocket in Native and Tyr19 Mutant High-Potential Iron Proteins by H-1-N-15 HMQC and F-19 NMR Experiments
The solvent accessibility of Chromatium vinosum high potential iron protein (HiPIP) has been investigated by use of H-1-N-15 HMQC, and F-19 NMR spectroscopy. These NMR experiments indicate that solvent accessibility to the cluster core is similar, and minimal, for the reduced and oxidized states of native HiPIP, but increases significantly for mutant proteins (Tyr19Leu and Tyr19His). These results support a proposed role [Agarwal, A.; Li, D.; Cowan, J. A. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 9440-9444] for Tyr19 in maintaining hydrolytic stability of the [Fe4S4] cluster, and demonstrate a general strategy for mapping out the solvent accessibility of protein-bound metalloredox prosthetic centers.