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

Heinz Jürgen Steinhoff, Ramin Mollaaghababa, Christian Altenbach, Kálmán Hideg, Mark Krebs, H. Gobind Khorana, Wayne L. Hubbell

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Abstract

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.

Original languageEnglish
Pages (from-to)105-107
Number of pages3
JournalScience
Volume266
Issue number5182
DOIs
Publication statusPublished - Oct 7 1994

ASJC Scopus subject areas

  • General

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    Steinhoff, H. J., Mollaaghababa, R., Altenbach, C., Hideg, K., Krebs, M., Khorana, H. G., & Hubbell, W. L. (1994). Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin. Science, 266(5182), 105-107. https://doi.org/10.1126/science.7939627