Abstract
Ultraviolet resonance Raman (UVRR) spectroscopy is a powerful technique for probing the structure of proteins. Vibrational scattering from different aromatic residues may be selectively enhanced by choosing appropriate excitation wavelengths. This raises the attractive possibility of using UVRR to study dynamic structural changes in proteins such as bacteriorhodopsin (BR), which functions as a light-driven proton pump. Indeed, the feasibility of UVRR experiments on BR has recently been demonstrated. It was previously proposed that light-adapted bacteriorhodopsin (BR{sub 568}) contains an ionized tyrosine (Tyr-185) which protonates upon light absorption and when the proton relaxes to its dark-adapted state (BR{sub DA}). The presence of tyrosinate in BR{sub 568} has also been suggested by recent UVVR experiments. In this communication, the authors present UVRR spectra of BR{sub 568} and BR{sub DA} which indicate that tyrosinate does not play a role in the photocycle.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
