Remenyi Christian, Reviakine Roman, Kaupp Martin
Institut für Anorganische Chemie, Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany.
J Phys Chem B. 2007 Jul 19;111(28):8290-304. doi: 10.1021/jp071745v. Epub 2007 Jun 26.
Modern density functional methods have been used to study spin-density distribution, g tensors, as well as Cu and ligand hyperfine tensors for azurin models, for two more blue copper proteins plastocyanin and stellacyanin, and for small model complexes. The aim was to establish a consistent computational protocol that provides a realistic description of the EPR parameters as probes of the spin-density distribution between metal and coordinated ligands in copper proteins. In agreement with earlier conclusions for plastocyanin, hybrid functionals with appreciable exact-exchange admixtures, roughly around 50%, provide the best overall agreement with all parameters. Then the bulk of the spin density is almost equally shared by the copper atom and the sulfur atom of the equatorial cysteine ligand, and the best values are obtained for copper, histidine nitrogen, and cysteine beta-proton hyperfine couplings, as well as for g(parallel). Spin-orbit effects on the EPR parameters may be appreciable and have to be treated carefully to obtain agreement with experiment. Most notably, spin-orbit effects on the (65)Cu hyperfine coupling tensors in blue copper sites are unusually large compared to more regularly coordinated Cu(II) complexes with similar spin density on copper. In addition to the often emphasized high covalency of the Cu-S(Cys) bond, the characteristically small A(parallel) component of blue copper proteins is shown to derive to a large part from a near-cancellation between negative first-order (Fermi contact and dipolar) and unusually large positive second-order (spin-orbital) contributions. The large spin-orbit effects relate to the distorted tetrahedral structures. Square planar dithiolene complexes with similar spin density on copper exhibit much more negative A(parallel) values, as the cancellation between nonrelativistic and spin-orbit contributions is less complete. Calculations on a selenocysteine-substituted variant of azurin have provided further insight into the relations between bonding and EPR parameters.
现代密度泛函方法已被用于研究天青蛋白模型、另外两种蓝色铜蛋白质体蓝素和星蓝蛋白以及小型模型配合物的自旋密度分布、g张量以及铜和配体超精细张量。目的是建立一个一致的计算方案,该方案能提供对电子顺磁共振(EPR)参数的现实描述,以此作为铜蛋白中金属与配位配体之间自旋密度分布的探针。与之前对质体蓝素的结论一致,具有约50%可观精确交换混合的杂化泛函与所有参数总体上吻合最佳。此时,大部分自旋密度几乎由铜原子和赤道面半胱氨酸配体的硫原子平均共享,并且对于铜、组氨酸氮和半胱氨酸β-质子超精细耦合以及g(平行)得到了最佳值。自旋轨道对EPR参数的影响可能很显著,必须谨慎处理才能与实验结果相符。最值得注意的是,与铜上具有相似自旋密度的更规则配位的Cu(II)配合物相比,蓝色铜位点上自旋轨道对(65)Cu超精细耦合张量的影响异常大。除了经常强调的Cu-S(Cys)键的高共价性外,蓝色铜蛋白特有的小A(平行)分量在很大程度上源于负的一阶(费米接触和偶极)与异常大的正二阶(自旋轨道)贡献之间的近乎抵消。大的自旋轨道效应与扭曲的四面体结构有关。在铜上具有相似自旋密度的平面二硫烯配合物表现出更负的A(平行)值,因为非相对论和自旋轨道贡献之间的抵消不太完全。对天青蛋白的硒代半胱氨酸取代变体的计算进一步深入了解了键合与EPR参数之间的关系。