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- W2926997944 abstract "We report the in vitro activity of recombinant BchC oxidoreductase involved in bacteriochlorophyll a biosynthesis. BchC of Rhodobacter capsulatus preferentially oxidizes 3 1 R ‐3‐(1‐hydroxyethyl)‐chlorophyllide a and 3 1 R ‐3‐(1‐hydroxyethyl)‐bacteriochlorophyllide a in the presence of NAD + to 3‐acetyl‐chlorophyllide a and bacteriochlorophyllide a , respectively, leaving the unreacted 3 1 S ‐epimers. In the reverse reaction, BchC with NADH predominately produces 3 1 R ‐epimeric alcohols from the 3‐acetyl‐(bacterio)chlorins. BchC of Chlorobaculum tepidum demonstrates the same 3 1 R ‐selectivity, suggesting that utilization of 3 1 R ‐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." @default.
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- W2926997944 date "2019-04-01" @default.
- W2926997944 modified "2023-10-16" @default.
- W2926997944 title "Stereoselective C3‐substituent modification and substrate channeling by oxidoreductase BchC in bacteriochlorophyll <i>a</i> biosynthesis" @default.
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- W2926997944 doi "https://doi.org/10.1002/1873-3468.13372" @default.
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