Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: covalent and nonlocal electrostatic contributions to reduction potentials.
作者： Ryan G Hadt , Ning Sun , Nicholas M Marshall , Keith O Hodgson , Britt Hedman
DOI: 10.1021/JA306438N
关键词: Magnetic circular dichroism 、 Covalent bond 、 Analytical chemistry 、 Electron paramagnetic resonance 、 Circular dichroism 、 Chemical physics 、 Chemistry 、 Azurin 、 Density functional theory 、 Resonance (chemistry) 、 Hydrogen bond
摘要: The reduction potentials (E0) of type 1 (T1) or blue copper (BC) sites in proteins and enzymes with identical first coordination spheres around the redox active ion can vary by ∼400 mV. Here, we use a combination low-temperature electronic absorption magnetic circular dichroism, electron paramagnetic resonance, resonance Raman, S K-edge X-ray spectroscopies to investigate series second-sphere variants—F114P, N47S, F114N Pseudomonas aeruginosa azurin—which modulate hydrogen bonding protein-derived dipoles nearby Cu–S(Cys) bond. Density functional theory calculations correlated experimental data allow for fractionation contributions tuning E0 into covalent nonlocal electrostatic components. These are found be significant, comparable magnitude, additive H-bonds, while passive H-bonds mostly nature. For dipoles, these terms oppose one another. This study provide...
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