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M104362200v1
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Papers In Press, published online ahead of print September 27, 2001
J. Biol. Chem, 10.1074/jbc.M104362200
Submitted on May 14, 2001
Revised on September 26, 2001
Accepted on September 27, 2001

Mimic of photocycle by a protein folding reaction in photoactive yellow protein

Byoung-Chul Lee, Paula A. Croonquist, and Wouter D. Hoff

Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637

Corresponding Author: whoff{at}midway.uchicago.edu

The blue light receptor photoactive yellow protein (PYP) displays rhodopsin-like photochemistry based on the trans to cis photoisomerization of its p-coumaric acid chromophore. Here, we report that protein refolding from the acid denatured state of PYP mimics the last photocycle transition in PYP. This implies a direct link between transient protein unfolding and photosensory signal transduction. We utilize this link to study general issues in protein folding. Chromophore trans to cis photoisomerization in the acid denatured state strongly decelerates refolding, and converts the pH dependence of the barrier for refolding from linear to non-linear. We propose transition state movement to explain this phenomenon. The cis chromophore significantly stabilizes the acid denatured state, but acidification of PYP results in the accumulation of the acid denatured state containing a trans chromophore. This provides a clear example of kinetic control in a protein unfolding reaction. These results demonstrate the power of PYP as a light-triggered model system to study protein folding.


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