Protein dynamics An overview on flash‐photolysis over broad temperature ranges

FEBS Letters

Di Iorio, Ernesto E.¹ 

[1] Laboratorium für Biochemie I, Eidgenössische Technische Hochshule, Universitätsstrasse 16, 8092 Zurich, Switzerland

关键词: Protein-dynamics;    Heme-protein;    Kinetics;    Flash-photolysis;    Protein-relaxation;    Low-temperature;   

DOI  :  10.1016/0014-5793(92)80893-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Ligand binding kinetics to heme-proteins between 40 and 300 K point to a regulatory role of protein dynamics. A protein-specific susceptibility of the heme-iron reactivity to dynamic fluctuations emerges from the distribution of reaction enthalpies derived from flash-photolysis measurements below ca. 180 K; we quantify it in terms of ‘intramolecular viscosity’, postulating that narrow low-temperature enthalpy distributions correspond to low internal viscosity and vice versa. The thermal evolution of ligand binding kinetics suggests, with other results, an interplay between high-frequency transitions of the amino acid side chains and low-frequency collective motions as a possible regulatory mechanism of protein dynamics.

【 授权许可】

Unknown