Further Studies with Isolated Absolute Infrared Spectra of Bacteriorhodopsin Photocycle Intermediates: Conformational Changes and Possible Role of a New Proton-Binding Center

$29.00 plus tax (Refund Policy)

Buy Article:


We recently published procedures describing the isolation of absolute infrared spectra for the intermediates of the bacteriorhodopsin (BR) photocycle and from these, obtaining transitional difference spectra between consecutive intermediates. In that work, we concentrated mainly on proton-binding centers and the route of proton transport across the membrane. In the current study, we used isolated spectra for the amide I, amide II, and amide III envelopes to obtain quantitative information on the extent of conformational change accompanying each transition in the photocycle. Our main finding was that most of the conformational changes occur in the conversion of the MF intermediate to N. In our earlier publication, a new proton acceptor, absorbing at 1650 cm−1 was identified, which appeared to accept a proton from Asp96COOH during the transformation of BR† to L. Below, we present evidence that supports this interpretation and propose a possible role for this new component.

Keywords: Amides I, II, and III; Conformational changes; FT-IR kinetics

Document Type: Research Article

DOI: http://dx.doi.org/10.1366/12-06662

Affiliations: National Institutes of Health, Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA

Publication date: January 1, 2013

More about this publication?
Related content



Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more