期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 115, 期 25, 页码 8296-8303出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp2020269
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资金
- iOpenShell Center for Computational Studies of Electronic Structure and Spectroscopy of Open-Shell and Electronically Excited Species
- National Science Foundation through the CRIF:CRF [CHE-0625419, 0624602, 0625237, CHE-0951634]
- Russian Foundation for Basic Research [10-03-0085]
- [MK-64815.2010.4]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0624602, 0625237] Funding Source: National Science Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0951634] Funding Source: National Science Foundation
The effect of the protein environment on the electronic structure of the gas phase green fluorescent protein (GFP) chromophore is investigated by QM/MM (quantum mechanics/molecular mechanics) calculations. The protein has very small effect on the excitation energy of the bright absorbing and the lowest triplet states of the anionic GFP chromophore, deprotonated 4-hydroxybenzylidene-2,3-dimethylimidazolinone (HBDI) anion, however, it increases vertical detachment energy from 2.5 eV (gas-phase deprotonated HBDI anion) to 5.0 eV (solvated protein). We also investigated possible existence of the charge-transfer-to-solvent (CTTS) states associated with the GFP chromophore. Although precursors of such states appear in cluster calculations, a tightly packed structure of the protein prevents the formation of the CTTS states in this system. Motivated by a recently discovered new type of photoconversion, oxidative redding, we characterized the redox properties of GFP. The computed standard reduction potential of the anionic form of GFP is 0.47 V (for the GFP(center dot) + le -> GFP(-) reaction), and the reduction potential at physiological conditions (pH 7, T = 25 degrees C) is 0.06 V.
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