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Heterologous Expression of the bchM Gene Product from Rhodobacter capsulatus and Demonstration that it Encodes S-Adenosyl-L-Methionine: Mg-Protoporhyrin IX Methyltransferase
Journal of Bacteriology (1994)
  • David Bollivar, Illinois Wesleyan University
  • Ze-Yu Jiang
  • Carl E. Bauer
  • Samuel I. Beale
Abstract
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.
Disciplines
Publication Date
Fall September, 1994
Publisher Statement
Journal of Bacteriology is published by the American Society for Microbiology, http://www.asm.org/.
Citation Information
David Bollivar, Ze-Yu Jiang, Carl E. Bauer and Samuel I. Beale. "Heterologous Expression of the bchM Gene Product from Rhodobacter capsulatus and Demonstration that it Encodes S-Adenosyl-L-Methionine: Mg-Protoporhyrin IX Methyltransferase" Journal of Bacteriology Vol. 176 Iss. 17 (1994)
Available at: http://works.bepress.com/david_bollivar/7/