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• W1991048729 startingPage "12043" @default.
• W1991048729 abstract "The dynamics of electronic and thermal relaxation of the heme in myoglobin (Mb) have been determined from subpicosecond time-resolved near-IR absorbance spectra of photoexcited Mb. A broad, short-lived absorbance feature near 12 000 cm-1 (833 nm) was observed and assigned to an excited electronic state of the heme. The photoexcited heme relaxes to its ground electronic state with a time constant of 3.4 ± 0.4 ps, leading to an absorbance spectrum that is indicative of a “hot” heme. The ensuing thermal relaxation was characterized by probing the spectral evolution of band III, a porphyrin−iron charge-transfer transition near 13 110 cm-1 (763 nm) that is sensitive to temperature. The temperature of the electronically relaxed heme cools exponentially with a time constant of 6.2 ± 0.5 ps. The implications of electronic and thermal relaxation to photolysis studies of liganded heme proteins are discussed." @default.
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• W1991048729 date "1996-01-01" @default.
• W1991048729 modified "2023-10-16" @default.
• W1991048729 title "Femtosecond Near-IR Absorbance Study of Photoexcited Myoglobin: Dynamics of Electronic and Thermal Relaxation" @default.
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• W1991048729 doi "https://doi.org/10.1021/jp9536458" @default.
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