Open AccessBiosynthesis of open‐chain tetrapyrroles in Prochlorococcus marinus
Author(s) -
Dammeyer Thorben,
Michaelsen Kristin,
FrankenbergDinkel Nicole
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2007.00715.x
Subject(s) - prochlorococcus , tetrapyrrole , phycobilisome , biology , complementation , synechococcus , cyanobacteria , biochemistry , mutant , gene , genetics , enzyme , bacteria
Members of the genus Prochlorococcus belong to the most abundant phytoplankton on earth. In contrast to other cyanobacteria, Prochlorococcus is characterized by divinyl‐chlorophyll containing light‐harvesting complexes and the lack of phycobilisomes. Despite the lack of phycobilisomes, all sequenced genomes of Prochlorococcus possess genes that putatively encode enzymes involved in the biosynthesis of open‐chain tetrapyrrole molecules. Here, biochemical evidence is presented indicating that high‐light‐ and low‐light‐adapted Prochlorococcus ecotypes possess genes encoding functional enzymes for the biosynthesis of open‐chain tetrapyrrole molecules. Experiments on recombinant protein as well as through complementation studies of a cyanobacterial insertion mutant revealed the functionality of the bilin reductases investigated.