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Science 7 October 1994:
Vol. 266. no. 5182, pp. 105 - 107
DOI: 10.1126/science.7939627
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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.


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