PMID:12437964

Citation	Watanabe, M, Matsui, T, Sasakura, Y, Sagami, I and Shimizu, T (2002) Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: effect of Met95 mutations. Biochem. Biophys. Res. Commun. 299:169-72
Abstract	In order to understand heme environment of a heme-regulated phosphodiesterase (Ec DOS), the binding behavior of cyanide to the Fe (III) complex was examined. Interestingly, the rate of cyanide binding to full-length Ec DOS was unusually slow with k(on)=0.0022mM(-1)s(-1), while the rate for the isolated heme domain of Ec DOS (0.045mM(-1)s(-1)) was 20-fold higher. Ala and Leu mutations at Met95, which has been suggested to be a heme axial ligand, increased the k(on) rate 11- and 8-fold, respectively, and dramatically decreased the cyanide dissociation rate from the isolated heme domain. His mutation at Met95, on the other hand, caused a 17-fold decrease in the k(on) value. We discuss the unusual cyanide binding behavior and the role of Met95 in controlling cyanide binding.
Links	PubMed
Keywords	Azides/metabolism; Cyanides/metabolism; Escherichia coli/enzymology; Fluorides/metabolism; Heme/metabolism; Imidazoles/metabolism; Iron/metabolism; Kinetics; Methionine/genetics; Mutagenesis, Site-Directed; Mutation; Phosphoric Diester Hydrolases/chemistry; Phosphoric Diester Hydrolases/genetics; Phosphoric Diester Hydrolases/metabolism; Protein Binding; Protein Structure, Tertiary; Spectrophotometry
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