Unveiling the Timescale of the R-T Transition in Human Hemoglobin

作者：Cammarata M; Levantino M; Wulff M; Cupane A^*

来源：Journal of Molecular Biology, 2010, 400(5): 951-962.

DOI：10.1016/j.jmb.2010.05.057

• hemoglobin
• allostery
• protein dynamics

Time-resolved wide-angle X-ray scattering, a recently developed technique allowing to probe global structural changes of proteins in solution, was used to investigate the kinetics of R-T quaternary transition in human hemoglobin and to systematically compare it to that obtained with time-resolved optical spectroscopy under nearly identical experimental conditions. Our data reveal that the main structural rearrangement associated with the R-T transition takes place similar to 2 mu s after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20-mu s step observed with time-resolved optical spectroscopy corresponds to a small and localized structural change.

• 出版日期2010-7-30