Literature DB >> 3140817

Evidence for light-induced lysine conformational changes during the primary event of the bacteriorhodopsin photocycle.

E McMaster1, A Lewis.   

Abstract

Fourier transform infrared difference spectroscopy is used to examine the role of lysine in the primary event of the bacteriorhodopsin photocycle. Isotopically labeled lysine is used to tentatively assign the lysine modes in the BR and K species. The results suggest that the lysine side-chain undergoes conformational changes in concert with the known light-induced chromophore structural alterations.

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Year:  1988        PMID： 3140817     DOI： 10.1016/s0006-291x(88)80808-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  4 in total

Review 1.  FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model.

Authors:  K J Rothschild
Journal:  J Bioenerg Biomembr       Date:  1992-04       Impact factor: 2.945

2.  Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.

Authors:  Joel E Morgan; Ahmet S Vakkasoglu; Janos K Lanyi; Johan Lugtenburg; Robert B Gennis; Akio Maeda
Journal:  Biophys J       Date:  2012-08-08       Impact factor: 4.033

3.  Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochemistry.

Authors:  Y Gat; M Grossjean; I Pinevsky; H Takei; Z Rothman; H Sigrist; A Lewis; M Sheves
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-15       Impact factor: 11.205

4.  Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy.

Authors:  Joel E Morgan; Ahmet S Vakkasoglu; Johan Lugtenburg; Robert B Gennis; Akio Maeda
Journal:  Biochemistry       Date:  2008-10-07       Impact factor: 3.162
  4 in total

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