高潜能 C112D/M121X（X = M、E、H、L）铜绿假单胞菌天青蛋白。
High-potential C112D/M121X (X = M, E, H, L) Pseudomonas aeruginosa azurins.
机构信息
Beckman Institute, California Institute of Technology, Pasadena, California 91125, USA.
出版信息
Inorg Chem. 2009 Feb 16;48(4):1278-80. doi: 10.1021/ic802322e.
Abstract
Site-directed mutagenesis of Pseudomonas aeruginosa azurin C112D at the M121 position has afforded a series of proteins with elevated Cu(II/I) reduction potentials relative to the Cu(II) aquo ion. The high potential and low axial hyperfine splitting (Cu(II) electron paramagnetic resonance A( parallel)) of the C112D/M121L protein are remarkably similar to features normally associated with type 1 copper centers.
摘要
对铜绿假单胞菌天青蛋白 C112D 进行 M121 位的定点突变，得到了一系列相对于 Cu(II)水合离子具有更高 Cu(II/I)还原电位的蛋白质。C112D/M121L 蛋白的高电位和低轴向超精细分裂（Cu(II)电子顺磁共振 A(平行)）与通常与 1 型铜中心相关的特征非常相似。
相似文献
1
High-potential C112D/M121X (X = M, E, H, L) Pseudomonas aeruginosa azurins.
Inorg Chem. 2009 Feb 16;48(4):1278-80. doi: 10.1021/ic802322e.
2
Spin delocalization over type zero copper.
Inorg Chem. 2012 Apr 2;51(7):4066-75. doi: 10.1021/ic202336m. Epub 2012 Mar 20.
3
Outer-sphere effects on reduction potentials of copper sites in proteins: the curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin.
J Am Chem Soc. 2010 Oct 20;132(41):14590-5. doi: 10.1021/ja105731x.
4
Modification of the electron-transfer sites of Pseudomonas aeruginosa azurin by site-directed mutagenesis.
FEBS Lett. 1989 Dec 4;258(2):266-8. doi: 10.1016/0014-5793(89)81670-9.
5
Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6.
FEBS Lett. 1996 Sep 23;394(1):87-90. doi: 10.1016/0014-5793(96)00934-9.
6
Type-zero copper proteins.
Nat Chem. 2009 Dec;1(9):711-5. doi: 10.1038/nchem.412.
7
Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids.
J Am Chem Soc. 2003 Jul 23;125(29):8760-8. doi: 10.1021/ja029699u.
8
Environment of copper in Pseudomonas aeruginosa azurin probed by binding of exogenous ligands to Met121X (X = Gly, Ala, Val, Leu, or Asp) mutants.
Biochemistry. 1996 Feb 20;35(7):2429-36. doi: 10.1021/bi9522110.
9
Transforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation.
J Am Chem Soc. 2010 Jul 28;132(29):10093-101. doi: 10.1021/ja102632p.
10
Electron transfer reactivity of type zero Pseudomonas aeruginosa azurin.
J Am Chem Soc. 2011 Apr 6;133(13):4865-73. doi: 10.1021/ja1093919. Epub 2011 Mar 15.
引用本文的文献
1
Unexpected effect of an axial ligand mutation in the type 1 copper center in small laccase: structure-based analyses and engineering to increase reduction potential and activity.
Chem Sci. 2025 May 19. doi: 10.1039/d5sc02177d.
2
Increasing Reduction Potentials of Type 1 Copper Center and Catalytic Efficiency of Small Laccase from Streptomyces coelicolor through Secondary Coordination Sphere Mutations.
Angew Chem Int Ed Engl. 2023 Dec 21;62(52):e202314019. doi: 10.1002/anie.202314019. Epub 2023 Nov 23.
3
Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins.
J Am Chem Soc. 2022 Mar 9;144(9):4178-4185. doi: 10.1021/jacs.1c13454. Epub 2022 Feb 16.
4
A Binuclear Cu Center Designed in an All α-Helical Protein Scaffold.
J Am Chem Soc. 2020 Aug 12;142(32):13779-13794. doi: 10.1021/jacs.0c04226. Epub 2020 Jul 29.
5
Prediction of Reduction Potentials of Copper Proteins with Continuum Electrostatics and Density Functional Theory.
Chemistry. 2017 Nov 2;23(61):15436-15445. doi: 10.1002/chem.201702901. Epub 2017 Sep 21.
6
Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Chem Rev. 2014 Apr 23;114(8):4366-469. doi: 10.1021/cr400479b.
7
Modulating the Copper-Sulfur Interaction in Type 1 Blue Copper Azurin by Replacing Cys112 with Nonproteinogenic Homocysteine.
Inorg Chem Front. 2014 Feb 1;1(2):153-158. doi: 10.1039/C3QI00096F.
8
Protein design: toward functional metalloenzymes.
Chem Rev. 2014 Apr 9;114(7):3495-578. doi: 10.1021/cr400458x. Epub 2014 Mar 24.
9
Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin.
Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):924-9. doi: 10.1073/pnas.1316483111. Epub 2014 Jan 3.
10
Tryptophan-accelerated electron flow across a protein-protein interface.
J Am Chem Soc. 2013 Oct 16;135(41):15515-25. doi: 10.1021/ja406830d. Epub 2013 Oct 2.
本文引用的文献
1
Electron Tunneling through Pseudomonas aeruginosa Azurins on SAM Gold Electrodes.
Inorganica Chim Acta. 2008 Mar 3;361(4):1095-1099. doi: 10.1016/j.ica.2007.08.022.
2
Establishing the entatic state in folding metallated Pseudomonas aeruginosa azurin.
Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3159-64. doi: 10.1073/pnas.0611149104. Epub 2007 Feb 14.
3
Reduction potential tuning of the blue copper center in Pseudomonas aeruginosa azurin by the axial methionine as probed by unnatural amino acids.
J Am Chem Soc. 2006 Dec 13;128(49):15608-17. doi: 10.1021/ja062732i.
4
Spectroscopic methods in bioinorganic chemistry: blue to green to red copper sites.
Inorg Chem. 2006 Oct 2;45(20):8012-25. doi: 10.1021/ic060450d.
5
Mimicking protein-protein electron transfer: voltammetry of Pseudomonas aeruginosa azurin and the Thermus thermophilus Cu(A) domain at omega-derivatized self-assembled-monolayer gold electrodes.
J Am Chem Soc. 2004 Nov 3;126(43):13954-61. doi: 10.1021/ja047875o.
6
The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin.
J Am Chem Soc. 2004 Jun 16;126(23):7244-56. doi: 10.1021/ja031821h.
7
Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins.
Chem Rev. 2004 Feb;104(2):419-58. doi: 10.1021/cr0206317.
8
Single-crystal EPR study at 95 GHz of the type 2 copper site of the inhibitor-bound quercetin 2,3-dioxygenase.
Biophys J. 2003 Dec;85(6):4047-54. doi: 10.1016/S0006-3495(03)74818-8.
9
Quantitative analysis of dinuclear manganese(II) EPR spectra.
J Magn Reson. 2003 Nov;165(1):33-48. doi: 10.1016/j.jmr.2003.07.001.
10
Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids.
J Am Chem Soc. 2003 Jul 23;125(29):8760-8. doi: 10.1021/ja029699u.
Zotero 插件