氰化物对血红素酶的抑制作用远不止于仅仅作为活性位点配体。
Cyanide does more to inhibit heme enzymes, than merely serving as an active-site ligand.
作者信息
Parashar Abhinav, Venkatachalam Avanthika, Gideon Daniel Andrew, Manoj Kelath Murali
机构信息
Center for Biomedical Research, VIT University, Vellore, Tamil Nadu, 632014 India.
REDOx Lab, PSG Institute of Advanced Studies, Avinashi Road, Peelamedu, Coimbatore, Tamil Nadu, 641004, India.
出版信息
Biochem Biophys Res Commun. 2014 Dec 12;455(3-4):190-3. doi: 10.1016/j.bbrc.2014.10.137. Epub 2014 Nov 6.
The toxicity of cyanide is hitherto attributed to its ability to bind to heme proteins' active site and thereby inhibit their activity. It is shown herein that the long-held interpretation is inadequate to explain several observations in heme-enzyme reaction systems. Generation of cyanide-based diffusible radicals in heme-enzyme reaction milieu could shunt electron transfers (by non-active site processes), and thus be detrimental to the efficiency of oxidative outcomes.
迄今为止，氰化物的毒性被认为是由于其能够与血红素蛋白的活性位点结合，从而抑制其活性。本文表明，长期以来的这种解释不足以解释血红素酶反应系统中的一些观察结果。在血红素酶反应环境中产生基于氰化物的可扩散自由基可能会使电子转移分流（通过非活性位点过程），从而对氧化反应的效率产生不利影响。
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