Low-frequency vibrations and their role in ultrafast photoisomerization reaction dynamics of photoactive yellow protein

Article Abstract:

Low-frequency vibrational modes of the native photoactive yellow protein (PYP) and its several mutant and analogue systems are investigated in "time" and "frequency" domains to elucidate their role in ultrafast photoisomerization reaction dynamics of PYP. A qualitative model called "trigger mode mediated guidance" is proposed to explain in simple terms the ultrafast primary process initiating PYP's photocycle.

Isomerization, Phosphoproteins

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Structural changes during the photocycle of photoactive yellow protein monitored by ultraviolet resonance Raman spectra of tyrosine and tryptophan

Article Abstract:

The ultraviolet resonance Raman (UVRR) spectra of photoactive yellow protein (PYP) excitations reported were investigated with protein structural changes accompanying the formation of putative signaling state, which denoted PYP(sub M). Several features that arise from changes in tyrosine and tryptophan vibrational modes exist in the difference spectra between PYP(sub dark) and PYP(sub M).

Analysis, Usage, Protein structure, Tryptophan, Tyrosine, Chemical properties

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Assignment of resonance Raman spectrum of photoactive yellow protein in its long-lived blue-shifted intermediate

Article Abstract:

The resonance Raman investigation of PYP(sub M) in solution at room temperature is presented. Raman spectroscopy is useful in studying photocycle mechanisms in PYP.

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