The functional role of the structure of the dioxo-isobacteriochlorin in the catalytic site of cytochrome cd₁ for the reduction of nitrite.

ABSTRACT: Cytochrome cd₁ is a key enzyme in bacterial denitrification and catalyzes one-electron reduction of nitrite (NO₂^-) to nitric oxide (NO) at the heme d₁ center under anaerobic conditions. The heme d₁ has a unique dioxo-isobacteriochlorin structure and is present only in cytochrome cd₁. To reveal the functional role of the unique heme d₁ in the catalytic nitrite reduction, we studied effect of the porphyrin macrocycle on each reaction step of the catalytic cycle of cytochrome cd₁ using synthetic model complexes. The complexes investigated are iron complexes of dioxo-octaethylisobacteriochlorin (1), mono-oxo-octaethylchlorin (2) and octaethylporphyrin (3). We show here that the reductio

SUBMITTER: Fujii H 

PROVIDER: S-EPMC6054029 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature