Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10220-10226 ◽  
Author(s):  
Roberto Barbato ◽  
Giulia Friso ◽  
Maria Teresa Giardi ◽  
Fernanda Rigoni ◽  
Giorgio Mario Giacometti
2007 ◽  
Vol 19 (4) ◽  
pp. 1347-1361 ◽  
Author(s):  
Xuwu Sun ◽  
Lianwei Peng ◽  
Jinkui Guo ◽  
Wei Chi ◽  
Jinfang Ma ◽  
...  

1990 ◽  
Vol 45 (5) ◽  
pp. 395-401 ◽  
Author(s):  
Susana Shochat ◽  
Noam Adir ◽  
Alma Gal ◽  
Yorinao Inoue ◽  
Laurence Mets ◽  
...  

Abstract The effect of unoccupancy of the QB site by plastoquinone on the photoinactivation of reaction center II in a Cyt b6/f-less mutant of Chlamydomonas reinhardtii, B6, was investigated. In these cells the oxidation of plastoquinol generated by electron flow via RC II to plastoquinone and thus the turnover of PQH2/PQ via the QB site are drastically reduced. Reaction center II of the mutant cells was resistant to photoinactivation relative to the control cells as demonstrated by measurements of light-induced destabilization of S2-QB charge recombination, rise in in­ trinsic fluorescence and loss of variable fluorescence. These parameters relate to functions in­ volving the reaction center II D1 protein. The light-induced degradation of D1 in the mutant cells was also considerably reduced, with a t 1/2 value of 7 h as compared, under similar conditions, to about 1.5 h for the control cells. These results indicate that the photoinactivation of RC II and turnover of the D1 protein are related and require occupancy of the QB site by PQ and its light-driven reduction.


1999 ◽  
Vol 274 (33) ◽  
pp. 23270-23275 ◽  
Author(s):  
Yoshihiro Narusaka ◽  
Mari Narusaka ◽  
Kimiyuki Satoh ◽  
Hirokazu Kobayashi

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