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F434Y mutant of AsLOV2

Candidate: toolkit item1 source documents6 linked claims
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Aliases

F434Y mutant, F434Y point mutation

Evidence Snippets

Phe434 is more than 6 Å from the FMN chromophore in AsLOV2; nevertheless, an F434Y point mutation is likely to change several structural features of the chromophore binding site
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1comparative photodynamicssupports2011Source 1DOIPubMed

Compared with wild-type AsLOV2, the F434Y mutant has significantly altered photodynamics.

Quoted textsource-backed
Transient absorption signals spanning 15 decades in time were compared for wild-type AsLOV2 and the F434Y mutant, showing that the latter has significantly altered photodynamics
Claim 2kinetic changesupports2011Source 1DOIPubMed

The F434Y mutant shows biphasic adduct-state formation kinetics on a microsecond time scale.

Quoted textsource-backed
(ii) biphasic formation of adduct-state kinetics on the microsecond time scale
Claim 3kinetic changesupports2011Source 1DOIPubMed

The F434Y mutant shows faster intersystem crossing leading to triplet formation on a nanosecond time scale.

Quoted textsource-backed
(i) a faster intersystem crossing leading to triplet formation on a nanosecond time scale
Claim 4kinetic changesupports2011Source 1DOIPubMed

The F434Y mutant shows greatly accelerated ground-state recovery kinetics on a second time scale.

Quoted textsource-backed
(iii) greatly accelerated ground-state recovery kinetics on a second time scale
Claim 5mechanistic effectsupports2011Source 1DOIPubMed

The F434Y mutation in AsLOV2 is likely to change several structural features of the chromophore binding site.

Quoted textsource-backed
an F434Y point mutation is likely to change several structural features of the chromophore binding site, as we demonstrate using molecular dynamics simulations
Claim 6mechanistic modelsupports2011Source 1DOIPubMed

The spectroscopic differences between wild-type AsLOV2 and the F434Y mutant are linked to changes in the configuration of the critical cysteine residue and to the chromophore's accessibility to solvent and oxygen.

Quoted textsource-backed
We present mechanistic models that link these spectroscopic differences to changes in the configuration of the critical cysteine residue and in the chromophore's accessibility to solvent and oxygen according to MD trajectories and purging experiments.