Primary steps of the photoactive yellow protein: isolated chromophore dynamics and protein directed function.
The cycle of the photoactive yellow protein (PYP) has been extensively studied, but the dynamics of the isolated chromophore responsible for transduction is unknown. Here, we present real-time observation of the dynamics of the negatively charged chromophore and detection of intermediates along the path of trans-to-cis isomerization using femtosecond mass selection/electron detachment techniques. The results show that the role of the protein environment is not in the first step of double-bond twisting (barrier crossing) but in directing efficient conversion to the cis-structure and in impeding radical formation within the protein.
Lee
I-Ren
IR
Arthur Amos Noyes Laboratory of Chemical Physics, Laboratory for Molecular Sciences, California Institute of Technology, Pasadena, CA 91125, USA.
Lee
Wonchul
W
Zewail
Ahmed H
AH
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D003116:Color; D020607:Halorhodospira halophila / Q000737:chemistry*; D008958:Models, Molecular; D010777:Photochemistry; D017434:Protein Structure, Tertiary; D013057:Spectrum Analysis
D001426:Bacterial Proteins