Prior to the decay of the relaxed fluorescent state (FS or I state), the protein is activated via a mechanism that does not require double bond isomerization. Most plausibly, it is a result of charge delocalization in the excited state of the polyene (or other) chromophores.
First-pass extracted concept
charge-delocalization-based early activation mechanism in bacteriorhodopsin
Candidate: concept label1 source documents5 linked claims
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Supporting Sources
Linked Claims
Appropriately bound chromophores can induce structural changes in proteins and other macromolecules upon optical excitation, potentially altering chemical reactivity.
Quoted textsource-backed
More generally, it is concluded that proteins and other macromolecules may undergo structural changes (that may affect their chemical reactivity) following optical excitation of an appropriately (covalently or non-covalently) bound chromophore.
Charge-delocalization-associated changes and C13=C14 isomerization-associated changes may couple during the bacteriorhodopsin photocycle, and their combination may drive cross-membrane proton pumping.
Quoted textsource-backed
It is suggested that the two effects may couple at a certain stage of the photocycle, and it is the combination of the two that drives the cross-membrane proton pump mechanism.
In bacteriorhodopsin, initial relaxation out of the Franck-Condon state does not involve substantial C13=C14 torsional motion and is considerably catalyzed by the protein matrix.
Quoted textsource-backed
It is concluded that in bR the initial relaxation out of the Franck-Condon (FC) state does not involve substantial C13=C14 torsional motion and is considerably catalyzed by the protein matrix.
Protein activation in bacteriorhodopsin can begin before decay of the relaxed fluorescent state through a mechanism that does not require double-bond isomerization.
Quoted textsource-backed
Prior to the decay of the relaxed fluorescent state (FS or I state), the protein is activated via a mechanism that does not require double bond isomerization.
The non-isomerization-dependent early activation mechanism in bacteriorhodopsin is most plausibly due to charge delocalization in the excited state of the chromophore.
Quoted textsource-backed
Most plausibly, it is a result of charge delocalization in the excited state of the polyene (or other) chromophores.