蓝色铜蛋白中的核磁共振超精细位移：量子化学研究。
NMR hyperfine shifts in blue copper proteins: a quantum chemical investigation.
作者信息
Zhang Yong, Oldfield Eric
机构信息
Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
出版信息
J Am Chem Soc. 2008 Mar 26;130(12):3814-23. doi: 10.1021/ja075978b. Epub 2008 Mar 4.
Abstract
We present the results of the first quantum chemical investigations of 1H NMR hyperfine shifts in the blue copper proteins (BCPs): amicyanin, azurin, pseudoazurin, plastocyanin, stellacyanin, and rusticyanin. We find that very large structural models that incorporate extensive hydrogen bond networks, as well as geometry optimization, are required to reproduce the experimental NMR hyperfine shift results, the best theory vs experiment predictions having R2 = 0.94, a slope = 1.01, and a SD = 40.5 ppm (or approximately 4.7% of the overall approximately 860 ppm shift range). We also find interesting correlations between the hyperfine shifts and the bond and ring critical point properties computed using atoms-in-molecules theory, in addition to finding that hyperfine shifts can be well-predicted by using an empirical model, based on the geometry-optimized structures, which in the future should be of use in structure refinement.
摘要
我们展示了对蓝铜蛋白（BCP）：腈蓝蛋白、天青蛋白、假天青蛋白、质体蓝素、星蓝蛋白和锈蓝蛋白中1H NMR超精细位移的首次量子化学研究结果。我们发现，需要非常大的结构模型，其中包含广泛的氢键网络以及几何优化，才能重现实验性NMR超精细位移结果，理论与实验的最佳预测具有R2 = 0.94、斜率 = 1.01和标准差 = 40.5 ppm（约占总体约860 ppm位移范围的4.7%）。除了发现可以使用基于几何优化结构的经验模型很好地预测超精细位移外，我们还发现超精细位移与使用分子中的原子理论计算的键和环临界点性质之间存在有趣的相关性，这在未来的结构优化中应该会有用处。
相似文献
1
NMR hyperfine shifts in blue copper proteins: a quantum chemical investigation.蓝色铜蛋白中的核磁共振超精细位移：量子化学研究。
J Am Chem Soc. 2008 Mar 26;130(12):3814-23. doi: 10.1021/ja075978b. Epub 2008 Mar 4.
2
Quantum chemical calculation of type-1 cu reduction potential: ligand interaction and solvation effect.量子化学计算 Cu1 型还原电势：配体相互作用与溶剂化效应。
J Phys Chem A. 2009 Nov 19;113(46):12979-87. doi: 10.1021/jp905825q.
3
Density functional study of EPR parameters and spin-density distribution of azurin and other blue copper proteins.蓝铜蛋白及其他蓝色铜蛋白的电子顺磁共振参数和自旋密度分布的密度泛函研究
J Phys Chem B. 2007 Jul 19;111(28):8290-304. doi: 10.1021/jp071745v. Epub 2007 Jun 26.
4
Active site structures and the redox properties of blue copper proteins: atomic resolution structure of azurin II and electronic structure calculations of azurin, plastocyanin and stellacyanin.蓝铜蛋白的活性位点结构与氧化还原特性：天青蛋白II的原子分辨率结构以及天青蛋白、质体蓝素和漆树蓝蛋白的电子结构计算
Dalton Trans. 2006 Jul 7(25):3067-76. doi: 10.1039/b513942b. Epub 2006 Feb 23.
5
Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin.通过¹H NMR光谱研究蓝色铜蛋白中的金属-配体相互作用：Cu(II)-假天青蛋白和Cu(II)-锈色氧化还原蛋白。
J Am Chem Soc. 2002 Nov 20;124(46):13698-708. doi: 10.1021/ja0267019.
6
A magnetic and electronic circular dichroism study of azurin, plastocyanin, cucumber basic protein, and nitrite reductase based on time-dependent density functional theory calculations.基于含时密度泛函理论计算的蓝蛋白、质体蓝素、黄瓜碱性蛋白和亚硝酸盐还原酶的磁圆二色性和电子圆二色性研究。
J Phys Chem A. 2010 Jun 3;114(21):6308-21. doi: 10.1021/jp101372s.
7
Functionally specified protein signatures distinctive for each of the different blue copper proteins.
BMC Bioinformatics. 2004 Sep 9;5:127. doi: 10.1186/1471-2105-5-127.
8
Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR study of Co(II)-pseudoazurin.受扰蓝铜位点中的金属-配体相互作用：钴（II）-假蓝铜蛋白的顺磁氢核磁共振研究
J Biol Inorg Chem. 2003 Jan;8(1-2):75-82. doi: 10.1007/s00775-002-0390-y. Epub 2002 Aug 29.
9
Protonation of type-1 Cu bound histidines: a quantum chemical study.质子化的第 1 型 Cu 键合组氨酸：量子化学研究。
Inorg Chem. 2010 Jan 18;49(2):435-44. doi: 10.1021/ic9012735.
10
Analysis of the paramagnetic copper(II) site of amicyanin by 1H NMR spectroscopy.通过核磁共振氢谱对氨腈蓝蛋白的顺磁性铜（II）位点进行分析。
Biochemistry. 1996 Mar 5;35(9):3085-92. doi: 10.1021/bi9518508.
引用本文的文献
1
Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.锰和钴在血红素铜氧化酶超家族生物合成模型的非血红素金属结合部位通过氧化还原非活性机制赋予氧化酶活性。
J Am Chem Soc. 2017 Sep 6;139(35):12209-12218. doi: 10.1021/jacs.7b05800. Epub 2017 Aug 25.
2
Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases.为什么在血红素铜氧化酶中，铜比铁更适合用于氧的激活和还原。
Nat Chem. 2017 Mar;9(3):257-263. doi: 10.1038/nchem.2643. Epub 2016 Nov 7.
3
Solid-state ¹⁷O NMR spectroscopy of paramagnetic coordination compounds.顺磁性配位化合物的固态¹⁷O核磁共振光谱学。
Angew Chem Int Ed Engl. 2015 Apr 13;54(16):4753-7. doi: 10.1002/anie.201409888. Epub 2015 Feb 18.
4
Computational investigations of HNO in biology.生物中 HNO 的计算研究。
J Inorg Biochem. 2013 Jan;118:191-200. doi: 10.1016/j.jinorgbio.2012.09.023. Epub 2012 Oct 5.
5
NMR, IR/Raman, and structural properties in HNO and RNO (R = alkyl and aryl) metalloporphyrins with implication for the HNO-myoglobin complex.NMR、IR/Raman 和 HNO 和 RNO（R = 烷基和芳基）金属卟啉的结构性质及其对 HNO-肌红蛋白复合物的影响。
J Am Chem Soc. 2010 Feb 10;132(5):1583-91. doi: 10.1021/ja907342s.
6
Mössbauer, NMR, geometric, and electronic properties in S = 3/2 iron porphyrins.S = 3/2铁卟啉中的穆斯堡尔效应、核磁共振、几何结构和电子性质
J Am Chem Soc. 2009 May 13;131(18):6386-8. doi: 10.1021/ja9006723.
7
Deciphering the NMR fingerprints of the disordered system with quantum chemical studies.通过量子化学研究破译无序系统的核磁共振指纹图谱。
J Phys Chem A. 2009 May 21;113(20):5993-7. doi: 10.1021/jp9001324.
本文引用的文献
1
Reduction potential tuning of the blue copper center in Pseudomonas aeruginosa azurin by the axial methionine as probed by unnatural amino acids.通过非天然氨基酸探测铜绿假单胞菌天青蛋白中轴向甲硫氨酸对蓝色铜中心还原电位的调节
J Am Chem Soc. 2006 Dec 13;128(49):15608-17. doi: 10.1021/ja062732i.
2
Solid-state NMR, crystallographic, and computational investigation of bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes.双膦酸盐及法尼基二磷酸合酶-双膦酸盐复合物的固态核磁共振、晶体学及计算研究
J Am Chem Soc. 2006 Nov 15;128(45):14485-97. doi: 10.1021/ja061737c.
3
Solid-state NMR of a paramagnetic DIAD-FeII catalyst: sensitivity, resolution enhancement, and structure-based assignments.顺磁性DIAD-FeII催化剂的固态核磁共振：灵敏度、分辨率增强及基于结构的归属
J Am Chem Soc. 2006 Oct 18;128(41):13545-52. doi: 10.1021/ja063510n.
4
Spectroscopic methods in bioinorganic chemistry: blue to green to red copper sites.生物无机化学中的光谱方法：从蓝色铜位点到绿色铜位点再到红色铜位点
Inorg Chem. 2006 Oct 2;45(20):8012-25. doi: 10.1021/ic060450d.
5
The role of hydrogen bonding at the active site of a cupredoxin: the Phe114Pro azurin variant.铜蓝蛋白活性位点处氢键的作用：苯丙氨酸114突变为脯氨酸的天青蛋白变体
Biochemistry. 2006 Jul 25;45(29):8812-22. doi: 10.1021/bi0606851.
6
QM/MM calculations with DFT for taking into account protein effects on the EPR and optical spectra of metalloproteins. Plastocyanin as a case study.采用密度泛函理论（DFT）的量子力学/分子力学（QM/MM）计算，以考虑蛋白质对金属蛋白电子顺磁共振（EPR）和光谱的影响。以质体蓝素为例进行研究。
J Comput Chem. 2006 Sep;27(12):1463-75. doi: 10.1002/jcc.20426.
7
Active site structures and the redox properties of blue copper proteins: atomic resolution structure of azurin II and electronic structure calculations of azurin, plastocyanin and stellacyanin.蓝铜蛋白的活性位点结构与氧化还原特性：天青蛋白II的原子分辨率结构以及天青蛋白、质体蓝素和漆树蓝蛋白的电子结构计算
Dalton Trans. 2006 Jul 7(25):3067-76. doi: 10.1039/b513942b. Epub 2006 Feb 23.
8
Detecting transient intermediates in macromolecular binding by paramagnetic NMR.通过顺磁核磁共振检测大分子结合中的瞬态中间体
Nature. 2006 Apr 27;440(7088):1227-30. doi: 10.1038/nature04673.
9
Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties.对锈蓝蛋白及其两个突变体的原子分辨率晶体结构、扩展X射线吸收精细结构（EXAFS）和量子化学研究揭示了其独特性质。
Biochemistry. 2006 Mar 7;45(9):2927-39. doi: 10.1021/bi052372w.
10
Determination of the geometric structure of the metal site in a blue copper protein by paramagnetic NMR.通过顺磁核磁共振确定蓝铜蛋白中金属位点的几何结构。
Proc Natl Acad Sci U S A. 2006 Feb 7;103(6):1738-43. doi: 10.1073/pnas.0507179103. Epub 2006 Jan 30.
Zotero 插件