Light-Induced and Thermal Relaxation in a Protein

Autor:	R. M. Ernst, G. U. Nienhaus, J. R. Mourant, Robert Philipp, Hans Frauenfelder, K. Chu
Rok vydání:	1995
Předmět:	Quantitative Biology::Biomolecules Materials science Photodissociation General Physics and Astronomy chemistry.chemical_compound Myoglobin chemistry Chemical physics Spectral hole burning Relaxation (physics) Absorption (chemistry) Excitation Visible spectrum Carbon monoxide
Zdroj:	Physical Review Letters. 74:2607-2610
ISSN:	1079-7114 0031-9007
DOI:	10.1103/physrevlett.74.2607
Popis:	After photodissociation of carbon monoxide bound to myoglobin, a thermally driven conformational relaxation towards the equilibrium structure of the deligated protein occurs above 160 K. Here we show that a relaxation can already be induced at lower temperatures by absorption of visible light. Both thermally induced and light-induced relaxations occur in discrete steps. The light-induced relaxation is characterized by a broad distribution of quantum yields. Similarities to spectral hole burning of dyes in glassy matrices suggest that the light-induced protein relaxation is initiated by electronic excitation of the heme group.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e3b10b58cc1e7a306556f8ff0724ab0 https://doi.org/10.1103/physrevlett.74.2607 Zobrazit plný text záznamu