Spin-forbidden CO ligand recombination in myoglobin
Spin-forbidden CO ligand recombination in myoglobin
复制标题
DOI：
10.1039/b314768a
复制
发表时间：
2004-01-01
影响因子：
3.4
通讯作者：
Harvey, JN
中科院分区：
文献类型：
--
作者：
Harvey, JN
血红素蛋白（如肌红蛋白）远端口袋内的小配体反应形成连接的低自旋铁复合物是生物无机化学中典型的自旋禁止过程，因为初始的“脱氧”铁复合物具有高自旋基态。密度泛函理论（DFT），过渡态理论（TST），和混合DFT/分子力学（QM/MM）计算的一氧化碳反应的报告。使用DFT数据的模型化合物，在室温下进行TST速率计算，得到公平的协议与实验，并建议高度非绝热性质的反应。QM/MM计算的整个蛋白质的报告，这是在定性协议的气相模型的结果，但建议蛋白质基质的反应速率的影响可能是重要的。
The reaction of small ligands within the distal pocket of haem proteins such as myoglobin, to form ligated, low-spin iron complexes is an archetypal spin-forbidden process in bioinorganic chemistry, because the initial, "deoxy'' iron complex has a high-spin ground state. Density functional theory (DFT), transition-state theory (TST), and hybrid DFT/molecular mechanics (QM/MM) calculations are reported on the carbon monoxide reaction. Using DFT data for a model compound, TST rate calculations at room temperature are carried out which give fair agreement with experiment, and suggest a highly non-adiabatic nature to the reaction. QM/MM calculations on the whole protein are reported, which are in qualitative agreement with the gas-phase model results, but suggest that protein matrix effects on the reaction rate may be important.