This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Burke, D H Articles by Hearst, J E Search for Related Content PubMed PubMed Citation Articles by Burke, D H Articles by Hearst, J E

 Previous Article  |  Next Article 

J Bacteriol. 1993 April; 175(8): 2414-2422

research-article

bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants.

Department of Chemistry, University of California, Berkeley.

ABSTRACT

We present the nucleotide and deduced amino acid sequences of four contiguous bacteriochlorophyll synthesis genes from Rhodobacter capsulatus. Three of these genes code for enzymes which catalyze reactions common to the chlorophyll synthesis pathway and therefore are likely to be found in plants and cyanobacteria as well. The pigments accumulated in strains with physically mapped transposon insertion mutations are analyzed by absorbance and fluorescence spectroscopy, allowing us to assign the genes as bchF, bchN, bchB, and bchH, in that order. bchF encodes a bacteriochlorophyll alpha-specific enzyme that adds water across the 2-vinyl group. The other three genes are required for portions of the pathway that are shared with chlorophyll synthesis, and they were expected to be common to both pathways. bchN and bchB are required for protochlorophyllide reduction in the dark (along with bchL), a reaction that has been observed in all major groups of photosynthetic organisms except angiosperms, where only the light-dependent reaction has been clearly established. The purple bacterial and plant enzymes show 35% identity between the amino acids coded by bchN and chlN (gidA) and 49% identity between the amino acids coded by bchL and chlL (frxC). Furthermore, bchB is 33% identical to ORF513 from the Marchantia polymorpha chloroplast. We present arguments in favor of the probable role of ORF513 (chlB) in protochlorophyllide reduction in the dark. The further similarities of all three subunits of protochlorophyllide reductase and the three subunits of chlorin reductase in bacteriochlorophyll synthesis suggest that the two reductase systems are derived from a common ancestor.

This article has been cited by other articles:

• Brocker, M. J., Virus, S., Ganskow, S., Heathcote, P., Heinz, D. W., Schubert, W.-D., Jahn, D., Moser, J. (2008). ATP-driven Reduction by Dark-operative Protochlorophyllide Oxidoreductase from Chlorobium tepidum Mechanistically Resembles Nitrogenase Catalysis. J. Biol. Chem. 283: 10559-10567 [Abstract] [Full Text]  
• Nomata, J., Mizoguchi, T., Tamiaki, H., Fujita, Y. (2006). 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. J. Biol. Chem. 281: 15021-15028 [Abstract] [Full Text]  
• Cheng, Y. S., Brantner, C. A., Tsapin, A., Collins, M. L. P. (2000). Role of the H Protein in Assembly of the Photochemical Reaction Center and Intracytoplasmic Membrane in Rhodospirillum rubrum. J. Bacteriol. 182: 1200-1207 [Abstract] [Full Text]  
• Fujita, Y., Bauer, C. E. (2000). Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits. IN VITRO CONFIRMATION OF NITROGENASE-LIKE FEATURES OF A BACTERIOCHLOROPHYLL BIOSYNTHESIS ENZYME. J. Biol. Chem. 275: 23583-23588 [Abstract] [Full Text]