通过激光光解研究蚯蚓血红蛋白的氧结合反应。
Hemerythrin's oxygen-binding reaction studied by laser photolysis.
作者信息
Alberding N, Lavalette D, Austin R H
出版信息
Proc Natl Acad Sci U S A. 1981 Apr;78(4):2307-9. doi: 10.1073/pnas.78.4.2307.
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.
摘要
氧合蚯蚓血红蛋白中的双氧-铁键被证明具有光敏性。光解离后的重组反应强烈依赖于溶剂粘度。在水中（η = 1厘泊或1×10⁻³帕·秒），重组是单相的，且在溶剂氧浓度上是二级反应，双分子速率系数为2.9×10⁷ M⁻¹ s⁻¹。在甘油/水混合物（η = 180厘泊）中也观察到了浓度依赖性的双分子复合过程。这为通过闪光光解研究一类蛋白质开辟了道路。
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