Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase

• DOI: 10.1128/jb.176.17.5290-5296.1994
• Publication Date: 2016-11-07T21:42:30Z
• Authors: D W Bollivar; Z Y Jiang; C E Bauer; S I Beale
• Keywords: Rhodobacter; Protoporphyrin IX; O-methyltransferase; Hemin

The bacteriochlorophyll biosynthesis gene, bchM, from Rhodobacter capsulatus was previously believed to code for a polypeptide involved in formation of the cyclopentone ring protochlorophyllide Mg-protoporphyrin IX monomethyl ester. In this study, R. bchM expressed Escherichia coli and gene product subsequently demonstrated by enzymatic analysis catalyze methylation form Activity required substrates S-adenosyl-L-methionine. 14C-labeled formed incubations containing 14C-methyl-labeled On basis these previous results, we also conclude that bchH which reported methyltransferase, is most likely Mg chelation step.