Sottini Silvia, Abbruzzetti Stefania, Viappiani Cristiano, Ronda Luca, Mozzarelli Andrea
Dipartimento di Fisica, Università degli Studi di Parma, Parco Area delle Scienze 7/A, Università degli Studi di Parma, Parco Area delle Scienze 23/A, 43100 Parma, Italy.
J Phys Chem B. 2005 Oct 20;109(41):19523-8. doi: 10.1021/jp054098l.
CO rebinding kinetics after nanosecond photolysis of myoglobin encapsulated in wet silica gels exhibits an enhanced geminate phase that allows the determination of the microscopic rate constants and the activation barriers for distinct ligand docking sites inside the protein matrix. Using a maximum entropy method, we demonstrate that the geminate phase can be well-described by a biphasic lifetime distribution, reflecting rebinding from the distal and proximal sites. Microscopic rates and activation barriers were estimated using a four-state model.
纳秒级光解封装在湿硅胶中的肌红蛋白后的一氧化碳再结合动力学表现出增强的双分子相，这使得能够确定蛋白质基质内不同配体对接位点的微观速率常数和活化能垒。使用最大熵方法，我们证明双分子相可以用双相寿命分布很好地描述，反映了从远端和近端位点的再结合。使用四态模型估计微观速率和活化能垒。
