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Hemerythrin's Oxygen-Binding Reaction Studied by Laser Photolysis

Neil Alberding, Daniel Lavalette and Robert H. Austin
Proceedings of the National Academy of Sciences of the United States of America
Vol. 78, No. 4, [Part2: Biological Sciences] (Apr., 1981), pp. 2307-2309
Stable URL: http://www.jstor.org/stable/10164
Page Count: 3
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Hemerythrin's Oxygen-Binding Reaction Studied by Laser Photolysis
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Abstract

The dioxygen-iron bond in oxyhemerythrin is shown to be photosensitive. The recombination reaction after photodissociation depends strongly on solvent viscosity. In water (η =1 centipoise or 1× 10-3 Pa· s) the recombination is monophasic and second-order in solvent oxygen concentration, with a bimolecular rate coefficient of 2.9× 107 M-1 s-1. In a glycerol/water mixture (η =180 centipoise) a concentration-dependent geminate recombination process is also seen. This opens a class of proteins to study by flash photolysis.

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