BciC‐Catalyzed C132‐Demethoxycarbonylation of Metal Pheophorbide a Alkyl Esters

Bacteriochlorophyll c molecules self‐aggregate to form large oligomers in the core part of chlorosomes, which are the main light‐harvesting antenna systems of green photosynthetic bacteria. In the biosynthetic pathway of bacteriochlorophyll c, a BciC enzyme catalyzes the removal of the C132‐methoxycarbonyl group of chlorophyllide a, which possesses a free propionate residue at the C17‐position and a magnesium ion as the central metal. The in vitro C132‐demethoxycarbonylations of chlorophyll a derivatives with various alkyl propionate residues and central metals were examined by using the BciC enzyme derived from one green sulfur bacteria species, Chlorobaculum tepidum. The BciC enzymatic reactions of zinc pheophorbide a alkyl esters were gradually suppressed with an increase of the alkyl chain length in the C17‐propionate residue (from methyl to pentyl esters) and finally the hexyl ester became inactive for the BciC reaction. Although not only the zinc but also nickel and copper complexes were demethoxycarbonylated by the BciC enzyme, the reactions were largely dependent on the coordination ability of the central metals: Zn>Ni>Cu. The above substrate specificity indicates that the BciC enzyme would not bind directly to the carboxy group of chlorophyllide a, but would bind to its central magnesium to form the stereospecific complex of BciC with chlorophyllide a, giving pyrochlorophyllide a, which lacks the (132R)‐methoxycarbonyl group. Removal service: In the biosynthesis of bacteriochlorophyll c, a BciC enzyme catalyzes removal of the C132‐methoxycarbonyl group of chlorophyllide a. In vitro BciC‐catalyzed demethoxycarbonylation reactions of metal pheophorbide a alkyl esters (chlorophyll a derivatives) are dependent on the alkyl chain length of C17 propionate residues and coordination ability of the central metals.