Hemerythrin's Oxygen-Binding Reaction Studied by Laser Photolysis

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 (η =1 centipoise or 1× 10-3Pa· s) the recombination is monophasic and second-order in solvent oxygen concentration, with a bimole...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1981-04, Vol.78 (4), p.2307-2309
Hauptverfasser: Alberding, Neil, Lavalette, Daniel, Austin, Robert H.
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Binding sites
Biochemistry
Hemeproteins
Hemerythrin - radiation effects
Kinetics
Lasers
Ligands
Metalloproteins - radiation effects
Oxygen
Photolysis
Protein Binding
Solvents
Viscosity
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Zusammenfassung: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× 10-3Pa· s) the recombination is monophasic and second-order in solvent oxygen concentration, with a bimolecular rate coefficient of 2.9× 107M-1s-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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.78.4.2307