Catalyses the transfer of a methyl group to the C-8 ethyl carbon in the biosynthesis of certain bacteriochlorophylls in Chlorobium tepidum, and has the sequence motif that tentatively assigns them to the cobalamin-dependent P-methylase subfamily.
Booker SJ
Anaerobic functionalization of unactivated C-H bonds
▸ Abstract
The functionalization of alkanes was once thought to lie strictly within the domain of enzymes that activate dioxygen in order to generate an oxidant with suitable potency to cleave inert C-H bonds. The emergence of the radical SAM superfamily of enzymes-those which use S-adenosyl-l-methionine as a precursor to a 5'-deoxyadenosyl 5'-radical-has kindled a renaissance in the study of radical-dependent enzymatic reactions, and is ushering in a wealth of new and intriguing chemistry that remains to be elucidated. This review will focus on a special subclass of radical SAM enzymes that functionalize inert C-H bonds, highlighting the functional groups and the chemistry that leads to their insertion. Within this class are first, enzymes that catalyze sulfur insertion, the prototype of which is biotin synthase; second, enzymes that catalyze P-methylation or C-methylation, such as P-methylase or Fom3; third, enzymes that catalyze oxygen insertion, such as the anaerobic magnesium protoporphyrin-IX oxidative cyclase (BchE); and fourth, enzymes that functionalize n-hexane or other alkanes as the first step in the metabolism of these inert compounds by certain bacteria. In addition to surveying reactions that have been studied at various levels of detail, this review will speculate on the mechanisms of other types of reactions that this chemistry lends itself to.
Bacteriochlorophyllide c C-8(2) and C-12(1) methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum
▸ Abstract
Bacteriochlorophyll (BChl) c is the major photosynthetic pigment in the green sulfur bacterium Chlorobaculum tepidum, in which it forms protein-independent aggregates that function in light harvesting. BChls c, d, and e are found only in chlorosome-producing bacteria and are unique among chlorophylls because of methylations that occur at the C-8(2) and C-12(1) carbons. Two genes required for these methylation reactions were identified and designated bchQ (CT1777) and bchR (CT1320). BchQ and BchR are members of the radical S-adenosylmethionine (SAM) protein superfamily; each has sequence motifs to ligate a [4Fe-4S] cluster, and we propose that they catalyze the methyl group transfers. bchQ, bchR, and bchQ bchR mutants of C. tepidum were constructed and characterized. The bchQ mutant produced BChl c that was not methylated at C-8(2), the bchR mutant produced BChl c that was not methylated at C-12(1), and the double mutant produced [8-ethyl, 12-methyl]-BChl c that lacked methylation at both the C-8(2) and C-12(1) positions. Compared to the wild type, the Qy absorption bands for BChl c in the mutant cells were narrower and blue shifted to various extents. All three mutants grew slower and had a lower cellular BChl c content than the wild type, an effect that was especially pronounced at low light intensities. These observations show that the C-8(2) and C-12(1) methylations of BChl c play important roles in the adaptation of C. tepidum to low light intensity. The data additionally suggest that these methylations also directly or indirectly affect the regulation of the BChl c biosynthetic pathway.
Chlorophyll biosynthesis in bacteria: the origins of structural and functional diversity
▸ Abstract
The use of photochemical reaction centers to convert light energy into chemical energy, chlorophototrophy, occurs in organisms belonging to only five eubacterial phyla: Cyanobacteria, Proteobacteria, Chlorobi, Chloroflexi, and Firmicutes. All chlorophototrophs synthesize two types of pigments: (a) chlorophylls and bacteriochlorophylls, which function in both light harvesting and uniquely in photochemistry; and (b) carotenoids, which function primarily as photoprotective pigments but can also participate in light harvesting. Although hundreds of carotenoids have been identified, only 12 types of chlorophylls (Chl a, b, d; divinyl-Chl a and b; and 8(1)-hydroxy-Chl a) and bacteriochlorophylls (BChl a, b, c, d, e, and g) are currently known to occur in bacteria. This review summarizes recent progress in the identification of genes and enzymes in the biosynthetic pathways leading to Chls and BChls, the essential tetrapyrrole cofactors of photosynthesis, and addresses the mechanisms for generating functional diversity for solar energy capture and conversion in chlorophototrophs.
Annu Rev Microbiol
2007;61(None):113-129
| PubMed ID:
17506685
