Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein.
Analysis of the chromophore p-coumaric acid, extracted from the ground state and the long-lived blue-shifted photocycle intermediate of photoactive yellow protein, shows that the chromophore is reversibly converted from the trans to the cis configuration, while progressing through the photocycle. The detection of the trans and cis isomers was carried out by high performance capillary zone electrophoresis and further substantiated by 1H NMR spectroscopy. The data presented here establish the photo-isomerization of the vinyl double bond in the chromophore as the photochemical basis for the photocycle of photoactive yellow protein, a eubacterial photosensory protein. A similar isomerization process occurs in the structurally very different sensory rhodopsins, offering an explanation for the strong spectroscopic similarities between photoactive yellow protein and the sensory rhodopsins. This is the first demonstration of light-induced isomerization of a chromophore double bond as the photochemical basis for photosensing in the domain of Bacteria.
Kort
R
R
Department of Microbiology, University of Amsterdam, The Netherlands.
Vonk
H
H
Xu
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X
Hoff
W D
WD
Crielaard
W
W
Hellingwerf
K J
KJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000528:radiation effects; D002841:Chromatiaceae / Q000737:chemistry; D003373:Coumaric Acids / Q000737:chemistry* / Q000528:radiation effects; D019075:Electrophoresis, Capillary; D007536:Isomerism; D009682:Magnetic Resonance Spectroscopy; D010777:Photochemistry; D020283:Photoreceptors, Microbial; D011422:Propionates; D011522:Protons; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D003373:Coumaric Acids; D020283:Photoreceptors, Microbial; D011422:Propionates; D011522:Protons; C050162:photoactive yellow protein, Bacteria; C495469:p-coumaric acid