Specific modification of tryptophan residues to N-formylkynurenine (NFK) occurs in the CP43 and D1 core polypeptides of PSII.
First-pass extracted concept
N-formylkynurenine
Candidate: concept label1 source documents6 linked claims
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Aliases
NFK
Evidence Snippets
Supporting Sources
Linked Claims
N-formylkynurenine accumulates in photosystem II during high light stress in vitro.
Quoted textsource-backed
NFK has been shown to accumulate in PSII during conditions of high light stress in vitro.
A speculative hypothesis discussed in the review is that N-formylkynurenine and other oxidative tryptophan modifications participate in the photosystem II damage and repair cycle.
Quoted textsource-backed
Also, the speculative hypothesis that NFK, and other oxidative modifications of tryptophan, play a role in the PSII damage and repair cycle is discussed.
N-formylkynurenine provides a marker for identifying reactive oxygen species generation sites in photosystem II and other proteins because of its unique optical and Raman signal.
Quoted textsource-backed
Owing to its unique optical and Raman signal, NFK provides a new marker to use in the identification of ROS generation sites in PSII and other proteins.
N-formylkynurenine formation is described as arising by a non-random, reactive-oxygen-species-targeted mechanism.
Quoted textsource-backed
The NFK modification has also been detected in other proteins, such as mitochondrial respiratory enzymes, and is formed by a non-random, ROS-targeted mechanism.
N-formylkynurenine modification of tryptophan occurs in the CP43 and D1 core polypeptides of photosystem II.
Quoted textsource-backed
Specific modification of tryptophan residues to N-formylkynurenine (NFK) occurs in the CP43 and D1 core polypeptides of PSII.
The role of reactive oxygen species in photoinhibition is under debate.
Quoted textsource-backed
Currently, the role of ROS in photoinhibition is under debate.