Hemerythrin's oxygen-binding reaction studied by laser photolysis.

N. Alberding; D. Lavalette; R. H. Austin

doi:10.1073/pnas.78.4.2307

Hemerythrin's oxygen-binding reaction studied by laser photolysis.

N. Alberding, D. Lavalette, R. H. Austin

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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 (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.

Original language	English (US)
Pages (from-to)	2307-2309
Number of pages	3
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	78
Issue number	4
DOIs	https://doi.org/10.1073/pnas.78.4.2307
State	Published - Apr 1981

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title = "Hemerythrin's oxygen-binding reaction studied by laser photolysis.",

abstract = "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.",

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year = "1981",

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AU - Lavalette, D.

AU - Austin, R. H.

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N2 - 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.

AB - 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.

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ER -

Hemerythrin's oxygen-binding reaction studied by laser photolysis.

Abstract

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