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.
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
PUBLICATION RECORD
- Publication year
2019
- Venue
FEBS Letters
- Publication date
2019-04-01
- Fields of study
Biology, Medicine, Chemistry, Environmental Science
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-20 of 20 references · Page 1 of 1
CITED BY
Showing 1-5 of 5 citing papers · Page 1 of 1