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This article shows that the activity of the protein kinase is regulated by the redox state of plastoquinone. We propose a
 

Summary:  This article shows that the activity of the protein kinase is
regulated by the redox state of plastoquinone. We propose a
molecular mechanism for state 1-state 2 transitions in vivo that
is consistent with these data and we argue that the presence of
cationsismerely a prerequisite forthese transitionsrather than a
decisive regulatory factor in itself.
Activation of the thylakoid protein b a s e
by light and reducing agents
The protein kinase activity of isolated thylakoids was assayed by
measuring the transfer of "P from [y-32P]ATP to total
membrane protein (Table 1).Light stimulated the kinase about
fourfold compared with a dark-incubated control. The herbicide
3-(3',4'-dichloropheny1)-l ,l-dimethylurea (DCMU), which
blocks electron transport between the primary acceptor (Q) of
photosystem I1 and plastoquinone, completely abolished the
stimulatory effect of light. The stimulation could not be restored
by addition of 2,6-dichlorophenolindophenol(DCPIP) in the
reduced form (DCPIPH2),which donates electrons to the inter-
system chain after plastoquinone. Thus, the kinase seemed to be
stimulated by reduction of certain intersystem electron carriers.

  

Source: Allen, John F. - School of Biological and Chemical Sciences, Queen Mary, University of London

 

Collections: Renewable Energy; Biology and Medicine