氧气和一氧化碳进入肌红蛋白的速率。
The rate of entry of dioxygen and carbon monoxide into myoglobin.
作者信息
Austin R H, Chan S S
出版信息
Biophys J. 1978 Oct;24(1):175-86. doi: 10.1016/S0006-3495(78)85354-5.
The model for carbon monoxide or dioxygen recombination with heme proteins developed by the group at the University of Illinois is reexamined. We propose that the carbon monoxide or dioxygen molecule enters the protein at essentially a diffusion-limited rate determined by the solvent viscosity and that the protein offers no important barriers to this entry. The viscosity dependence of the entry rate k(ED), its magnitude (1 x 10(10) M(-1)s(-1), and the rate of quenching of triplet states of protoprophyrin IX in apomyoglobin by dioxygen are used as supporting evidence. Comparison is made to the model of a fluctuating protein developed by G. Weber.
伊利诺伊大学研究小组所建立的一氧化碳或双氧基与血红素蛋白重组的模型被重新审视。我们认为，一氧化碳或双氧基分子以本质上由溶剂粘度决定的扩散限制速率进入蛋白质，并且蛋白质对这种进入没有重要障碍。进入速率k(ED)的粘度依赖性、其大小（1×10¹⁰ M⁻¹s⁻¹）以及双氧基对脱辅基肌红蛋白中原卟啉IX三重态的猝灭速率被用作支持证据。与G. 韦伯所建立的波动蛋白模型进行了比较。
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