Biochimica et Biophysica Acta (BBA) - Bioenergetics
Volume 1817, Issue 2, February 2012, Pages 287-297
Two functional sites of phosphatidylglycerol for regulation of reaction of plastoquinone QB in photosystem II
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Highlights
► Phosphatidylglycerol was depleted from cyanobacterial pgsA-gene-inactivated cells. ► Two PG molecules regulate activities of QB and oxygen evolution differently. ► Loss of high-affinity PGH inhibits QB directly and suppress intrinsic O2 evolution. ► Loss of low-affinity PGL enhances PSII affinity to BQ that inactivates QB. ► Binding sites of PGH and PGL in PS II structure are estimated.
Abbreviations
APC
allophycocyanin
BQ
p-benzoquinone
Chl
chlorophyll
D(BQ) and D2(int)
decay of fluorescence yield measured with and without BQ
DCMU
3-(3′,4′-dichlorophenyl)-1,1-dimethylurea
DGDG
digalactosyldiacylglycerol
MGDG
monogalactosyldiacylglycerol
O2(BQ) and O2(int)
oxygen evolution activity with and without BQ, respectively
PAM
pulse amplidue modulation
PC
phycocyanin
PG
phosphatidylglycerol
PGH and PGL
PG bound to the high- and low-affinity sites that regulate the QB function, respectively
PG1-5
PG molecules identified in the structure of PS II
PS
photosystem
QA and QB
first and second electron acceptor plastoquinoneof PSII
RC
reaction center
SQDG
sulfoquinovosyldiacyglycerol
WT
wild type
Keywords
Chlorophyll fluorescence
Lipid
Oxygen evolution
Phosphatidylglycerol
Photosystem II assembly
QB plastoquinone
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Present address: Genetic Research Center of Nagoya University, Furocyo, Chikusa, Nagoya 464-8602, Japan.
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