Kinetic evidence for three photolyzable taxonomic conformational substates in oxymyoglobin.
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.
Tetreau
Catherine
C
Institut Curie-Recherche, INSERM U350, Bâtiment 112, Centre Universitaire, 91405 Orsay, France.
Novikov
Eugene
E
Tourbez
Martine
M
Lavalette
Daniel
D
D000818:Animals; D007700:Kinetics; D008027:Light; D015233:Models, Statistical; D009211:Myoglobin / Q000737:chemistry*; D016011:Normal Distribution; D010100:Oxygen / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors; D014466:Ultraviolet Rays; D014907:Whales
D009211:Myoglobin; C017595:oxymyoglobin; D010100:Oxygen