Calculation of Resonance Raman Spectra and Excited State Properties for Blue Copper Protein Model Complexes
Calculation of Resonance Raman Spectra and Excited State Properties for Blue Copper Protein Model Complexes
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蓝铜蛋白模型复合物的共振拉曼光谱和激发态性质的计算
DOI：
10.1021/acssuschemeng.2c04802
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发表时间：
2022
影响因子：
8.4
通讯作者：
Korzeniewski, Carol
中科院分区：
文献类型：
--
作者：
Ozuguzel, Umut;Aquino, Adelia J.;Nieman, Reed;Minteer, Shelley D.;Korzeniewski, Carol
漆酶作为生态友好型生物燃料电池阴极催化剂的潜力已被广泛研究。在这些应用中，电子从电极直接转移到酶内所谓的1型（T1）氧化还原位点。多年来，共振拉曼（RR）光谱被用于探测配体与静止氧化形式漆酶和相关蓝铜蛋白T1位点Cu2+中心相互作用的性质。光谱解释是由小分子T1位点模拟物的平行研究指导的。本文报道了时间依赖密度泛函理论（TDDFT）计算的结果，这些计算是基于Cu2+硫酸盐配合物的T1位点模拟，这些配合物由三齿三（吡唑基）氢硼酸盐配体或双齿β-二酮酸配体稳定。计算了每个配合物的前10个重态的垂直激发能。所得的电子吸收光谱和红外光谱与实验结果吻合良好。红外光谱在400 cm-1附近以Cu-S强拉伸跃迁为主，该跃迁对硫酸盐配体内部的分子构象敏感。这些结果为建立漆酶催化活性位点的先进模型提供了基础，以支持可持续技术。
Laccase enzymes have been investigated for their potential as eco-friendly biofuel cell cathode catalysts. In these applications, electrons transfer from the electrode directly to the so-called Type 1 (T1) redox site within the enzyme. Over the years, resonance Raman (RR) spectroscopy has been utilized to probe the nature of ligand interactions with the Cu2+center at the T1 site of the resting, oxidized form of laccases and related blue copper proteins. Spectral interpretation has been guided by parallel studies of small molecule T1 site mimics. Reported herein are results of time-dependent density functional theory (TDDFT) calculations performed on a series of experimentally well-studied T1 site mimics based on Cu2+thiolate complexes stabilized by either a tridentate tris(pyrazolyl)hydroborate ligand or a bidentate β-diketiminate ligand. Vertical excitation energies were computed for the first 10 doublet states of each complex. The electronic absorption and RR spectra derived show excellent agreement with the experiment. RR spectra were dominated by a strong Cu–S stretching transition near 400 cm–1, which is sensitive to molecular conformation within the thiolate ligand. The results provide a foundation to build from in advancing models of laccase catalytic active sites in support of sustainable technologies.
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蓝铜蛋白的共振拉曼光谱：星花青蛋白和漆酶的正常模式计算以及 Copper-63/copper-65 和 H2O/D2O 位移的分配
影响因子：
2.9
作者：
L. Nestor;J. Larrabee;G. Woolery;B. Reinhammar;T. Spiro
通讯作者：
T. Spiro
影响因子：
14.9
作者：
wwPDB consortium
通讯作者：
wwPDB consortium
I 型铜蛋白配位基团的变化：34S、65Cu 和 15N 标记质体蓝蛋白的共振拉曼光谱
DOI：
--
发表时间：
1995
期刊：
影响因子：
--
作者：
D. Qiu;S. Dong;J. Ybe;M. Hecht;T. Spiro
通讯作者：
T. Spiro
“蓝色”铜蛋白的共振拉曼光谱及其铜位点的性质。
影响因子：
15
作者：
O. Siiman;N. Young;P. Carey
通讯作者：
P. Carey
影响因子：
8
作者：
Machczynski, MC;Vijgenboom, E;Canters, GW
通讯作者：
Canters, GW