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• W2034005337 abstract "Nanosecond time-resolved absorption and magnetic optical rotatory dispersion (MORD) measurements of photolyzed myoglobin−CO visible bands (500−650 nm) are presented. These measurements reveal a 400 ns process, spectrally distinct from ligand recombination, that accounts for 7% of the observed spectral evolution in the visible absorption bands and 4% in the MORD. The time-resolved MORD, more sensitive to heme coordination geometry than absorption, suggests that this process is most likely associated with protein relaxation on the distal side of the heme pocket, perhaps accompanying rehydration of the deoxymyoglobin photoproduct or accommodation of protein side chains to ligand escape." @default.
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• W2034005337 date "1998-11-19" @default.
• W2034005337 modified "2023-10-18" @default.
• W2034005337 title "Spectroscopic Evidence for Nanosecond Protein Relaxation after Photodissociation of Myoglobin−CO" @default.
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• W2034005337 doi "https://doi.org/10.1021/bi9814437" @default.
• W2034005337 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9860868" @default.
• W2034005337 hasPublicationYear "1998" @default.
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