Journal
NATURE CHEMISTRY
Volume 5, Issue 3, Pages 212-220Publisher
NATURE PORTFOLIO
DOI: 10.1038/NCHEM.1565
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Funding
- Research Center Program of Institute for Basic Science (IBS) in Korea [CA1201]
- Creative Research Initiatives (Center for Time-Resolved Diffraction) of MEST/NRF of Korea
- National Science Foundation [0952643, 0843459]
- National Institutes of Health (NIH) [GM036452]
- NIH National Institute of General Medical Sciences [P41GM103543]
- NIH/NIDDK through the Intramural Research Program of the NIDDK
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0952643] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0843459] Funding Source: National Science Foundation
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Trans-to-cis isomerization, the key reaction in photoactive proteins, usually cannot occur through the standard one-bond-flip mechanism. Owing to spatial constraints imposed by a protein environment, isomerization probably proceeds through a volume-conserving mechanism in which highly choreographed atomic motions are expected, the details of which have not yet been observed directly. Here we employ time-resolved X-ray crystallography to visualize the isomerization of the p-coumaric acid chromophore in photoactive yellow protein with a time resolution of 100 ps and a spatial resolution of 1.6 angstrom. The structure of the earliest intermediate (I-T) resembles a highly strained transition state in which the torsion angle is located halfway between the trans-and cis-isomers. The reaction trajectory of I-T bifurcates into two structurally distinct cis intermediates via hula-twist and bicycle-pedal pathways. The bifurcating reaction pathways can be controlled by weakening the hydrogen bond between the chromophore and an adjacent residue through E46Q mutation, which switches off the bicycle-pedal pathway.
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