Structural relaxation and nonexponential kinetics of CO-binding to horse myoglobin. Multiple flash photolysis experiments.

Abstract:

:The geminate recombination kinetics of CO-myoglobin strongly deviates from single exponential behavior in contrast to what is expected for unimolecular reactions (1). At low temperatures, this result was attributed to slowly exchanging conformational states which differ substantially in barrier height for ligand binding. Above 160 K the kinetics apparently slow down with temperature increase. Agmon and Hopfield (2) explain this result in terms of structural relaxation perpendicular to the reaction coordinate, which enhances the activation energy. In their model, structural relaxation homogenizes the kinetic response. Recently, Steinbach et al. (3) proposed a relaxation model which conserves the kinetic inhomogeneity. Below we test these conjectures by single and multiple excitation experiments. This method allows for discrimination between parallel (inhomogeneous) and sequential (homogeneous) kinetic schemes. The kinetic anomaly above 160 K is shown to result from a homogeneous, structurally relaxed intermediate. However a second anomaly is found above 210 K concerning the inhomogeneous phase which may indicate either a shift in activation energy or entropy.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Post F,Doster W,Karvounis G,Settles M

doi

10.1016/S0006-3495(93)81554-6

subject

Has Abstract

pub_date

1993-06-01 00:00:00

pages

1833-42

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(93)81554-6

journal_volume

64

pub_type

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