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• W1990008506 abstract "Phosphodiesterase (Ec DOS) from Escherichia coli is a gas-sensor enzyme in which binding of gas molecules, such as O2, CO, and NO, to the Fe(II)-protoporphyrin IX complex in the sensor domain stimulates phosphodiesterase activity toward cyclic-di-GMP. In this study, we report that external axial ligands, such as cyanide or imidazole, bind to Fe(III)-protoporphyrin IX in the sensor domain and induce a 10- to 11-fold increase (from 8.1 up to 86 min−1) in catalysis, which is more substantial than that (6.3 to 7.2-fold) observed for other gas-stimulated Fe(II) heme-bound enzymes. Catalytic activity (50 min−1) of the heme-free mutant, H77A, was comparable to that of the ligand-stimulated enzymes. Accordingly, we propose that the heme at the sensor domain inhibits catalysis and that ligand binding to the heme iron complex releases this catalytic suppression. Furthermore, mutations of Met95, Arg97, and Phe113 at the putative heme distal side suppressed the ligand effects on catalysis. The rate constants (19,000 × 10−5 μM−1min−1) for cyanide binding to the M95A and M95L mutants of the full-length enzyme were 633-fold higher than that to wild-type Ec DOS (30 × 10−5 μM−1min−1). The absorption spectrum of the F113Y mutant suggests that the Tyr O− group directly coordinates to the Fe(III) complex and that the cyanide binding rate to the mutant is very slow, compared with those of the wild-type and other mutant proteins. We observed a similar trend in the binding behavior of imidazole to full-length mutant enzymes. Therefore, while Met95 and Phe113 are not direct axial ligands for the Fe(III) complex, catalytic, spectroscopic, and ligand binding evidence suggests that these residues are located in the vicinity of the heme." @default.
• W1990008506 created "2016-06-24" @default.
• W1990008506 creator A5032672742 @default.
• W1990008506 creator A5046562567 @default.
• W1990008506 date "2008-11-18" @default.
• W1990008506 modified "2023-09-26" @default.
• W1990008506 title "Ligand Binding to the Fe(III)-Protoporphyrin IX Complex of Phosphodiesterase from <i>Escherichia coli</i> (<i>Ec</i> DOS) Markedly Enhances Catalysis of Cyclic di-GMP: Roles of Met95, Arg97, and Phe113 of the Putative Heme Distal Side in Catalytic Regulation and Ligand Binding" @default.
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• W1990008506 doi "https://doi.org/10.1021/bi8012017" @default.
• W1990008506 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19053256" @default.
• W1990008506 hasPublicationYear "2008" @default.
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