Stereoselective C3‐substituent modification and substrate channeling by oxidoreductase BchC in bacteriochlorophyll a biosynthesis

Misato Teramura,Y. Tsukatani,J. Harada,Mitsuaki Hirose,H. Tamiaki

Published 2019 in FEBS Letters

ABSTRACT

We report the in vitro activity of recombinant BchC oxidoreductase involved in bacteriochlorophyll a biosynthesis. BchC of Rhodobacter capsulatus preferentially oxidizes 31R‐3‐(1‐hydroxyethyl)‐chlorophyllide a and 31R‐3‐(1‐hydroxyethyl)‐bacteriochlorophyllide a in the presence of NAD+ to 3‐acetyl‐chlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S‐epimers. In the reverse reaction, BchC with NADH predominately produces 31R‐epimeric alcohols from the 3‐acetyl‐(bacterio)chlorins. BchC of Chlorobaculum tepidum demonstrates the same 31R‐selectivity, suggesting that utilization of 31R‐epimers in BchC‐catalyzed reductions may be conserved across different phyla of photosynthetic bacteria. Additionally, the presence of BchC accelerates the 3‐vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3‐acetyl‐chlorophyllide a through 3‐(1‐hydroxyethyl)‐chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis.

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