Computational studies of the primary phototransduction event in visual rhodopsin.
This Account addresses recent advances in the elucidation of the detailed molecular rearrangements due to the primary photochemical event in rhodopsin, a prototypical G-protein-coupled receptor (GPCR) responsible for the signal transmission cascade in the vertebrate vision process. The reviewed studies provide fundamental insight on long-standing problems regarding the assembly and function of the individual residues and bound water molecules that form the rhodopsin active site, a center that catalyzes the 11-cis/all-trans isomerization of the retinyl chromophore in the primary step of the phototransduction mechanism. Emphasis is placed on the authors' recent computational studies, based on state-of-the-art quantum mechanics/molecular mechanics (QM/MM) hybrid methods, addressing the structural refinement of the retinyl chromophore binding site in high-resolution X-ray structures of bovine visual rhodopsin, the energy storage mechanism, and the molecular origin of spectroscopic changes due to the primary photochemical event.
Gascón
José A
JA
Department of Chemistry, Yale University, P. O. Box 208107, New Haven, CT 06520-8107, USA.
Sproviero
Eduardo M
EM
Batista
Victor S
VS
D007536:Isomerism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012168:Retinal Pigments / Q000737:chemistry / Q000502:physiology*; D012243:Rhodopsin / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction
D012168:Retinal Pigments; D012243:Rhodopsin