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Science 17 October 1997:
Vol. 278. no. 5337, p. 361
DOI: 10.1126/science.278.5337.361j
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After reactions such as photodissociation of a ligand from the binding site of a protein, the protein is left with excess energy; it subsequently cools through redistribution of the vibrational energy and by dissipating energy into the surrounding water solvent. Mizutani et al. studied the relative contributions of these processes in the cooling of myoglobin after photodissociation of CO with picosecond time resolution. They obtained evidence for two time scales in the heme cooling, which they attribute to a classical diffusion process and a collective motion process.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)