Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 7 October 1994:
Vol. 266. no. 5182, pp. 105 - 107
DOI: 10.1126/science.7939627
Prev | Table of Contents | Next

Articles

Science, Vol 266, Issue 5182, 105-107
Copyright © 1994 by American Association for the Advancement of Science

articles

Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin

HJ Steinhoff, R Mollaaghababa, C Altenbach, K Hideg, M Krebs, HG Khorana, and WL Hubbell

Institut fur Biophysik, Ruhr-Universitat Bochum, Germany.

Bacteriorhodopsin was selectively spin labeled at residues 72, 101, or 105 after replacement of the native amino acids by cysteine. Only the electron paramagnetic resonance spectrum of the label at 101 was time-dependent during the photocycle. The spectral change rose with the decay of the M intermediate and fell with recovery of the ground state. The transient signal is interpreted as the result of movement in the C-D or E-F interhelical loop, or in both, coincident with protonation changes at the key aspartate 96 residue. These results link the optically characterized intermediates with localized conformational changes in bacteriorhodopsin during the photocycle.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Transmembrane Nitration of Hydrophobic Tyrosyl Peptides. LOCALIZATION, CHARACTERIZATION, MECHANISM OF NITRATION, AND BIOLOGICAL IMPLICATIONS.
H. Zhang, K. Bhargava, A. Keszler, J. Feix, N. Hogg, J. Joseph, and B. Kalyanaraman (2003)
J. Biol. Chem. 278, 8969-8978
   Abstract »    Full Text »    PDF »
Rational design of `water-soluble' bacteriorhodopsin variants.
K. Mitra, T. A. Steitz, and D. M. Engelman (2002)
Protein Eng. Des. Sel. 15, 485-492
   Abstract »    Full Text »    PDF »
Bioenergetics of the Archaea.
G. Schafer, M. Engelhard, and V. Muller (1999)
Microbiol. Mol. Biol. Rev. 63, 570-620
   Abstract »    Full Text »    PDF »
Structural Determinants for Agonist Binding Affinity to Thromboxane/Prostaglandin Endoperoxide (TP) Receptors. ANALYSIS OF CHIMERIC RAT/HUMAN TP RECEPTORS.
G. W. Dorn II, M. G. Davis, and D. D. D'Angelo (1997)
J. Biol. Chem. 272, 12399-12405
   Abstract »    Full Text »    PDF »
Electron diffraction studies of light-induced conformational changes in the Leu-93 right-arrow Ala bacteriorhodopsin mutant.
S. Subramaniam, A. R. Faruqi, D. Oesterhelt, and R. Henderson (1997)
PNAS 94, 1767-1772
   Abstract »    Full Text »    PDF »
Protein Conformational Changes during the Bacteriorhodopsin Photocycle.
A. Nilsson, P. Rath, J. Olejnik, M. Coleman, and K. J. Rothschild (1995)
J. Biol. Chem. 270, 29746-29751
   Abstract »    Full Text »    PDF »
Bacteriorhodpsin Experiences Light-induced Conformational Alterations in Nonisomerizable C13=C14 Pigments. A STUDY WITH EPR.
A. Aharoni, L. Weiner, M. Ottolenghi, and M. Sheves (2000)
J. Biol. Chem. 275, 21010-21016
   Abstract »    Full Text »    PDF »
Time-resolved x-ray diffraction reveals multiple conformations in the M-N transition of the bacteriorhodopsin photocycle.
T. Oka, N. Yagi, T. Fujisawa, H. Kamikubo, F. Tokunaga, and M. Kataoka (2000)
PNAS 97, 14278-14282
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)