Hemerythrin's oxygen-binding reaction studied by laser photolysis.
The dioxygen--iron bond in oxyhemerythrin is shown to be photosensitive. The recombination reaction after photodissociation depends strongly on solvent viscosity. In water (eta = 1 centipoise or 1 x 10(-3) Pa . s) the recombination is monophasic and second-order in solvent oxygen concentration, with a bimolecular rate coefficient of 2.9 x 10(7) M-1 s-1. In a glycerol/water mixture (eta = 180 centipoise) a concentration-dependent geminate recombination process is also seen. This opens a class of proteins to study by flash photolysis.
D000818:Animals; D006422:Hemerythrin / Q000528:radiation effects; D007700:Kinetics; D007834:Lasers; D008667:Metalloproteins / Q000528:radiation effects; D010100:Oxygen; D010782:Photolysis; D011485:Protein Binding
D006422:Hemerythrin; D008667:Metalloproteins; D010100:Oxygen