3-deacetyl-3-vinylbacteriochlorophyllide a [CPD:C18152];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
bacteriochlorophyllide a [CPD:C18155];
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a [CPD:C18153]
chlorophyllide a [CPD:C02139];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a [CPD:C18154]
The enzyme, together with EC 184.108.40.2066, bacteriochlorophyllide-a dehydrogenase, and EC 220.127.116.11, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 18.104.22.168, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) . The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 22.214.171.124), which catalyses an ATP-driven reduction.
EC 126.96.36.199 created 1965 as EC 188.8.131.52, modified 2012, transferred 2016 to EC 184.108.40.206
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.