Heme-regulated phosphodiesterase from
Escherichia coli (
Ec DOS) is a novel PAS heme-sensor enzyme.
Ec DOS is active in the Fe
2+ heme-bound form, whereas it is inactive in the Fe
3+ heme-bound form. To elucidate the mechanism of the redox-dependent heme-regulated catalysis, we examined spectroscopic and functional characters of site-directed and deletion mutant proteins. We also determined crystal structures of the wild type enzyme under various conditions. In this review, we summarized findings about heme-sensor proteins, PAS domain and phosphodiesterase in general and structure and function relationships of
Ec DOS specifically.
抄録全体を表示