Exploring the ability of chlorophyll b to bind to the CP43' protein induced under iron deprivation in a mutant of Synechocystis PCC 6803 containing the cao gene. Export

@article{Duncan2003, abstract = {Cyanobacteria, unlike plants and green algae, do not contain chlorophyll (Chl) b. This is because of the absence of the cao gene which encodes the enzyme that catalyses a two step oxygenation of chlorophyllide a to chlorophyllide b. Recently, however, the cao gene of higher plants was engineered into Synechocystis PCC 6803 leading to Chl b synthesis in this cyanobacterium [Satoh et al., J. Biol. Chem. 276 (2001) 4293-4297]. Here we use this same cao-plus mutant to show that Chl b can bind to the CP43' protein, expressed in cells exposed to low iron levels, which normally binds Chl a only. In so doing CP43' is changed to a Chl a/Chl b-binding protein and in this respect resembles the closely related Chl a/Chl b-binding Pcb protein of prochlorophytes (green oxyphotobacteria). The results emphasise the possibility of using an in vitro system to elucidate factors which control the binding of these two different forms of chlorophylls to the six transmembrane helical light-harvesting proteins of oxygenic photosynthetic organisms.}, author = {Duncan, J. and Bibby, T. and Tanaka, A. and Barber, J.}, citeulike-article-id = {4785379}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/12706839}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=12706839}, day = {24}, issn = {0014-5793}, journal = {FEBS letters}, keywords = {chlorophyll\_d}, month = {April}, number = {1-3}, pages = {171--175}, posted-at = {2009-06-09 10:26:00}, priority = {2}, title = {Exploring the ability of chlorophyll b to bind to the CP43' protein induced under iron deprivation in a mutant of Synechocystis PCC 6803 containing the cao gene.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12706839}, volume = {541}, year = {2003} }

TY - JOUR ID - Duncan2003 L3 - citeulike-article-id:4785379 N2 - Cyanobacteria, unlike plants and green algae, do not contain chlorophyll (Chl) b. This is because of the absence of the cao gene which encodes the enzyme that catalyses a two step oxygenation of chlorophyllide a to chlorophyllide b. Recently, however, the cao gene of higher plants was engineered into Synechocystis PCC 6803 leading to Chl b synthesis in this cyanobacterium [Satoh et al., J. Biol. Chem. 276 (2001) 4293-4297]. Here we use this same cao-plus mutant to show that Chl b can bind to the CP43' protein, expressed in cells exposed to low iron levels, which normally binds Chl a only. In so doing CP43' is changed to a Chl a/Chl b-binding protein and in this respect resembles the closely related Chl a/Chl b-binding Pcb protein of prochlorophytes (green oxyphotobacteria). The results emphasise the possibility of using an in vitro system to elucidate factors which control the binding of these two different forms of chlorophylls to the six transmembrane helical light-harvesting proteins of oxygenic photosynthetic organisms. IS - 1-3 JF - FEBS letters SN - 0014-5793 EP - 175 TI - Exploring the ability of chlorophyll b to bind to the CP43' protein induced under iron deprivation in a mutant of Synechocystis PCC 6803 containing the cao gene. VL - 541 SP - 171 KW - chlorophyll_d AU - Duncan, J AU - Bibby, T AU - Tanaka, A AU - Barber, J PY - 2003/04/24/ UR - http://view.ncbi.nlm.nih.gov/pubmed/12706839 ER -