Bacteriochlorophyll homolog compositions in the bchU mutants of green sulfur bacteria.
Photochem Photobiol Sci
; 12(12): 2195-201, 2013 Dec.
Article
in En
| MEDLINE
| ID: mdl-24145897
ABSTRACT
Chlorosomes of the green sulfur bacterium Chlorobaculum limnaeum contain a large number of self-aggregated bacteriochlorophyll (BChl) e molecules. The ΔbchU mutant of this organism lacks BchU, a C20-methyltransferase, and therefore produces BChl f, which is the C20-unsubstituted form of BChl e. The BChl e homolog compositions, in terms of degrees of C8(2)-methylation, were not changed in the wild type during growth, while the BChl f homolog patterns in the mutant were significantly altered at various time periods of growth. BChl f with an isobutyl group at the C8 position was dominant at the early stage of growth, whereas the proportion of BChl f with the C8-ethyl group increased in the late exponential phase. We also constructed the ΔbchU mutant of C. tepidum which originally produces BChl c the mutant therefore produces BChl d. BChl d homologs highly methylated at the C8(2) position also increased in the ΔbchU mutant of C. tedium compared to those in the wild type. These phenomena suggest that BchU interferes with the methylation ability of BchQ, a C8(2)-methyltransferase, and that the enzymes might compete in terms of obtaining S-adenosyl-methionine, the source of a methyl group. As a result, when grown to the late log phase, the ΔbchU mutant of C. limnaeum had similar heterogeneities of pigment homolog compositions compared to those in the wild type. Chlorosomes with a high proportion of C8-ethylated BChl homologs might be important for fine-tuning the light-harvesting or energy-transfer efficiency. Chlorosomes of the ΔbchU mutants at the various growth stages will be good materials for investigating effects of C8(2)-methylations on supramolecular structures of self-aggregated pigments.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Bacteriochlorophylls
/
Chlorobi
/
Methyltransferases
Language:
En
Journal:
Photochem Photobiol Sci
Journal subject:
BIOLOGIA
/
QUIMICA
Year:
2013
Document type:
Article