The light-induced inactivation of the photochemical reaction center II (RCII) of oxygenic chloroplasts (photoinhibition) was investigated
First-pass extracted concept
photochemical reaction center II
Candidate: toolkit item1 source documents8 linked claims
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Aliases
RCII, reaction center II
Evidence Snippets
Supporting Sources
Linked Claims
Photoinhibition of reaction center II is resolved into a reversible conformational change followed by an irreversible modification of the RCII D1 protein.
Quoted textsource-backed
The process is resolved into a reversible conformational change followed by an irreversible modification of RCII D1 protein.
In a fraction of RCII, electron donation from Z to P+680 was impaired without loss of primary photochemistry.
Quoted textsource-backed
the amplitude of signal II was reduced by 20-30%, indicating that in a fraction of RCII, electron donation from Z to P+680 was impaired without losing primary photochemistry.
The extent of charge separation P+680QA- was not affected by the light-induced modification.
Quoted textsource-backed
The extent of charge separation (P+680Q-A) was not affected.
The first reversible step is characterized by destabilization of the secondary acceptor semiquinone anion QB bound to the D1 protein.
Quoted textsource-backed
The first step is characterized by (i) destabilization of the secondary acceptor semiquinone anion, Q-B, bound to the D1 protein.
A change in QB stability could allow charge equilibration with QA and explain increased intrinsic fluorescence and reduced electron flow to plastoquinone.
Quoted textsource-backed
The change in the Q-B stability could allow charge equilibration with QA and thus explain the rise in the intrinsic fluorescence level and reduction of electron flow to plastoquinone.
The change in the lifetime of P+680 can account for further reduction in electron flow during photoinhibition.
Quoted textsource-backed
The change in the lifetime of P+680 can account for further reduction in electron flow (photo-inhibition).
The light-induced changes observed in vivo persisted in isolated thylakoids.
Quoted textsource-backed
The light-induced changes in vivo persisted in isolated thylakoids.
Unoccupancy of the QB site by plastoquinone partially protected RCII against light-induced destabilization of QB.
Quoted textsource-backed
Unoccupancy of the QB site by plastoquinone partially protected RCII against the light-induced destabilization of Q-B.