期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 12, 页码 5520-5523出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja3009117
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资金
- NIH at Kyoto [R01EY016400-04]
- CREST from JST
- NSF [MRI-R2, CHE-0958205]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0958205] Funding Source: National Science Foundation
Detailed knowledge of the molecular mechanisms that control the spectral properties in the rhodopsin protein family is important for understanding the functions of these photoreceptors and for the rational design of artificial photosensitive proteins. Here we used a high-level ab initio QM/MM method to investigate the mechanism of spectral tuning in the chloride-bound and anion-free forms of halorhodopsin from Natronobacterium pharaonis (phR) and the interprotein spectral shift between them. We demonstrate that the chloride ion tunes the spectral properties of phR via two distinct mechanisms: (i) electrostatic interaction with the chromophore, which results in a 95 nm difference between the absorption maxima of the two forms, and (ii) induction of a structural reorganization in the protein, which changes the positions of charged and polar residues and reduces this difference to 29 nm. The present study expands our knowledge concerning the role of the reorganization of the internal H-bond network for color tuning in general and provides a detailed investigation of the tuning mechanism in phR in particular.
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