Heterologous Expression of the bchM Gene Product from Rhodobacter capsulatus and Demonstration that it Encodes S-Adenosyl-L-Methionine: Mg-Protoporhyrin IX Methyltransferase

David Bollivar, Ze-Yu Jiang, Carl E. Bauer, Samuel I. Beale

Research output: Journal ArticleArticlepeer-review


The bacteriochlorophyll biosynthesis gene, bchM, from Rlodobacter capsulatus was previously believed to code for a polypeptide involved in formation of the cyclopentone ring of protochlorophyllide from Mg-protoporphyrin IX monomethyl ester. In this study, R. capsulatus bchM was expressed in Escherichia coli and the gene product was subsequently demonstrated by enzymatic analysis to catalyze methylation of Mg-protoporphyrin IX to form Mg-protoporphyrin IX monomethyl ester. Activity required the substrates Mg-protoporphyrin IX and S-adenosyl-L-methionine. 14C-labeled product was formed in incubations containing 14C-methyl-labeled S-adenosyl-L-methionine. On the basis of these and previous results, we also conclude that the bchH gene, which was previously reported to code for Mg-protoporphyrin IX methyltransferase, is most likely involved in the Mg chelation step.
Original languageAmerican English
JournalJournal of Bacteriology
StatePublished - Sep 1994


  • Molecular Biology

Cite this