Kinetic evidence for three photolyzable taxonomic conformational substates in oxymyoglobin

Biophysical Journal
C TetreauD Lavalette

Abstract

The kinetics of oxygen geminate binding with the taxonomic substates of MbO2 are reported. The maximum entropy method was used to analyze the rebinding kinetics of MbCO and MbO2 monitored in the Soret. The resulting rate distributions were found to consist of a small number of overlapping bands. A global parametric fit of a series of rate distributions recorded at several temperatures was performed using a Gaussian basis set to resolve the individual enthalpy distributions P(H). This approach was first validated by showing that the well-documented taxonomic substates of MbCO could be recovered. The method was then applied to MbO2. Three taxonomic substates were identified at pH 4.8, whereas only two of them contribute to oxygen geminate rebinding at pH 7.0. These findings show that, similarly to MbCO, MbO2 also exists as three photolyzable and kinetically different taxonomic substates and suggest reconsidering the issue of the photolysis quantum yield of MbO2.

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Citations

May 28, 2005·Biochimica Et Biophysica Acta·Catherine Tetreau, Daniel Lavalette
Jul 27, 2010·Biochimica Et Biophysica Acta·Karin Nienhaus, G Ulrich Nienhaus
Nov 11, 2008·Biochimica Et Biophysica Acta·Sergei V Lepeshkevich, Boris M Dzhagarov
Oct 19, 2004·Biophysical Journal·Catherine TetreauDaniel Lavalette
Dec 26, 2003·Biophysical Journal·Catherine TetreauDaniel Lavalette
Sep 1, 2017·Methods and Applications in Fluorescence·Eugene G NovikovAntonie J W G Visser

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