Fine Tuning of Structure and Reactivity of Copper Complexes Using Pyridylalkylamine Ligands — Active Site Models for Copper Proteins

ChemInform ◽  
2006 ◽  
Vol 37 (17) ◽  
Author(s):  
Shinobu Itoh
Keyword(s):  
Active Site ◽  
Copper Complexes ◽  
Fine Tuning ◽  
Copper Proteins

Fine Tuning of the Copper Active Site in Polysaccharide Monooxygenases

2020 ◽  
Vol 124 (10) ◽  
pp. 1859-1865
Author(s):  
Son Tung Ngo ◽  
Han N. Phan ◽  
Chinh N. Le ◽  
Nhung C. T. Ngo ◽  
Khanh Bao Vu ◽  
...  
Keyword(s):  
Active Site ◽  
Fine Tuning ◽  
Polysaccharide Monooxygenases

Fine-tuning the coordination atoms of copper redox mediators: an effective strategy for boosting the photovoltage of dye-sensitized solar cells

2019 ◽  
Vol 7 (20) ◽  
pp. 12808-12814 ◽  
Author(s):  
Yawei Zhao ◽  
Junyu Shen ◽  
Ze Yu ◽  
Maowei Hu ◽  
Chong Liu ◽  
...  
Keyword(s):  
Solar Cells ◽  
Copper Complexes ◽  
Dye Sensitized Solar Cells ◽  
Redox Mediator ◽  
Fine Tuning ◽  
Effective Strategy ◽  
Redox Mediators ◽  
New Class ◽  
Dye Sensitized ◽  
Sensitized Solar Cells

Herein, we report a new class of copper complexes bearing a tetradentate polythioether ligand, [(S4)Cu]2+/+ (12+/+, S4 = 1,4,8,11-tetrathiocyclotetradecane), as a redox mediator in dye-sensitized solar cells (DSCs).

The Electronic Properties of a Model Active Site for Blue Copper Proteins as Probed by Stark Spectroscopy

2002 ◽  
Vol 106 (11) ◽  
pp. 3007-3012 ◽  
Author(s):  
Arindam Chowdhury ◽  
Linda A. Peteanu ◽  
Patrick L. Holland ◽  
William B. Tolman
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Stark Spectroscopy ◽  
Blue Copper

H-Bonding Maintains the Active Site of Type 1 Copper Proteins:  Site-Directed Mutagenesis of Asn38 inPoplarPlastocyanin†

Biochemistry ◽  
1999 ◽  
Vol 38 (11) ◽  
pp. 3379-3385 ◽  
Author(s):  
Shoulian Dong ◽  
Joel A. Ybe ◽  
Michael H. Hecht ◽  
Thomas G. Spiro
Keyword(s):  
Active Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Copper Proteins ◽  
Type 1 Copper

Modeling the active site in hemocyanin: Synthesis and reactivity of binuclear copper complexes

1989 ◽  
Vol 166 (1) ◽  
pp. 71-77 ◽  
Author(s):  
Thomas N. Sorrell ◽  
Martha L. Garrity ◽  
Debora J. Ellis
Keyword(s):  
Active Site ◽  
Copper Complexes ◽  
Binuclear Copper

XRD and EXAFS studies of azomethynic copper metallochelates as models of blue copper proteins

2004 ◽  
Vol 19 (3) ◽  
pp. 225-231 ◽  
Author(s):  
V. G. Vlasenko ◽  
A. T. Shuvaev ◽  
A. L. Nivorozkin ◽  
A. I. Uraev
Keyword(s):  
Copper Complexes ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Lattice Space ◽  
Monoclinic Lattice ◽  
Ray Patterns ◽  
X Ray Absorption

The structure of two biomimetic copper complexes bis[4-benzylaldimino-3-methyl-1-phenyl-5-thio (seleno)pyrazolato]copper(II)—36 32N6X2Cu (where X=S, Se) have been studied and X-ray patterns of these compounds have been prepared using the Rietveld refinement technique. Both complexes crystallized in a monoclinic lattice, space group-C2/c(15). The unit-cell parameters are a=28.917(3) Å; b=7.000(2) Å; c=17.550(4) Å; β=106.869(1) (1) for C36H32CuN6S2 and a=29.126(6) Å; b=7.042(4) Å; c=17.228(2) Å; β=105.587(2) for C36H32CuN6Se2. Analysis of the copper and selenium K-edge X-ray absorption spectra (EXAFS) of these complexes show that a copper atom is in pseudo-tetrahedric ligand environment N2X2 with typical Cu–N bonds (R=2.00–2.01 Å) and significantly different Cu–S and Cu–Se bonds (R=2.27 Å and R=2.41 Å, respectively) because of different sulfur and selenium ion radii. © 2004 International Centre for Diffraction Data.

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