Journal
BIOCHEMISTRY
Volume 40, Issue 46, Pages 13788-13801Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi0107142
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Funding
- NCRR NIH HHS [RR07707] Funding Source: Medline
- NIGMS NIH HHS [GM36452] Funding Source: Medline
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The photocycle of the bacterial blue-light photoreceptor, photoactive yellow protein, was stimulated by illumination of single crystals by a 7 ns laser pulse. The molecular events were recorded at high resolution by time-resolved X-ray Laue diffraction as they evolved in real time, from I ns to seconds after the laser pulse. The complex structural changes during the photocycle at ambient temperature are displayed in a movie of difference electron density maps relative to the dark state. The step critical to entry into the photocycle is identified as flipping of the carbonyl group of the 4-hydroxycinnamic acid chromophore into an adjacent, hydrophobic environment rather than the concomitant isomerization about the double bond of the chromophore tail. The structural perturbation generated at the chromophore propagates throughout the entire protein as a light-induced protein quake with its epicenter at the carbonyl moiety of the chromophore.
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