Molecular dynamics simulations of cooling in laser-excited heme proteins.
Author(s) -
Eric R. Henry,
William A. Eaton,
Remo Hochstrasser
Publication year - 1986
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.83.23.8982
Subject(s) - myoglobin , heme , excited state , chromophore , chemistry , protein dynamics , raman spectroscopy , molecular dynamics , hemeprotein , non equilibrium thermodynamics , chemical physics , kinetics , absorption (acoustics) , recombination , atomic physics , photochemistry , physics , thermodynamics , optics , computational chemistry , biochemistry , organic chemistry , quantum mechanics , enzyme , gene
In transient optical experiments the absorbed photon raises the vibrational temperature of the chromophore. In heme proteins at room temperature conversion of a 530-nm photon into vibrational energy is estimated to raise the temperature of the heme by 500-700 K. Cooling of the heme is expected to occur mainly by interacting with the surrounding protein. We report molecular dynamics simulations for myoglobin and cytochrome c in vacuo that predict that this cooling occurs on the ps time scale. The decay of the vibrational temperature is nonexponential with about 50% loss occurring in 1-4 ps and with the remainder in 20-40 ps. These results predict the presence of nonequilibrium vibrational populations that would introduce ambiguity into the interpretation of transient ps absorption and Raman spectra and influence the kinetics of sub-ns geminate recombination.
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