scholarly journals Electrostatic Regulation of Blue Copper Sites

2021 ◽  
Author(s):  
Daniel Bím ◽  
Anastassia Alexandrova
Keyword(s):  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Local Perturbations ◽  
Copper Sites

In the last 50 years, the blue copper proteins became central targets of investigation. Extensive experiments focused on the Cu coordination to probe the effect of local perturbations on its...

scholarly journals Electrostatic Regulation of Blue Copper Sites

2021 ◽  
Author(s):  
Daniel Bím ◽  
Anastassia N. Alexandrova
Keyword(s):  
Electric Fields ◽  
Bond Distance ◽  
Fine Tuning ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Local Perturbations ◽  
Coordination Spheres ◽  
Bond Covalency ◽  
Geometric And Electronic Properties

<div> <p>In the last 50 years, the blue copper proteins became central targets of investigation. Extensive experiments focused on the first- and second-coordination spheres of Cu to probe the effect of local perturbations on its properties. We found that local electric fields, generated by charged residues evolutionarily placed throughout the protein edifice, constitute an additional significant factor regulating blue copper proteins. These fields are not random, but exhibit a highly specific directionality, negative with respect to Cu-S<sub>Cys</sub> and Cu-S<sub>Met</sub> in the Cu first shell. The field magnitude contributes to fine-tuning of the geometric and electronic properties of Cu sites in individual blue copper proteins. Specifically, the local electric fields evidently control the Cu-S<sub>Met</sub> bond distance, Cu(II)-S<sub>Cys</sub> bond covalency, and the energies of the frontier molecular orbitals, which, in turn, govern the Cu(II/I) reduction potential and the relative absorption intensities at 450 nm and 600 nm.</p> </div> <br>

scholarly journals Electrostatic Regulation of Blue Copper Sites

2021 ◽  
Author(s):  
Daniel Bím ◽  
Anastassia N. Alexandrova
Keyword(s):  
Electric Fields ◽  
Bond Distance ◽  
Fine Tuning ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Local Perturbations ◽  
Coordination Spheres ◽  
Bond Covalency ◽  
Geometric And Electronic Properties

<div> <p>In the last 50 years, the blue copper proteins became central targets of investigation. Extensive experiments focused on the first- and second-coordination spheres of Cu to probe the effect of local perturbations on its properties. We found that local electric fields, generated by charged residues evolutionarily placed throughout the protein edifice, constitute an additional significant factor regulating blue copper proteins. These fields are not random, but exhibit a highly specific directionality, negative with respect to Cu-S<sub>Cys</sub> and Cu-S<sub>Met</sub> in the Cu first shell. The field magnitude contributes to fine-tuning of the geometric and electronic properties of Cu sites in individual blue copper proteins. Specifically, the local electric fields evidently control the Cu-S<sub>Met</sub> bond distance, Cu(II)-S<sub>Cys</sub> bond covalency, and the energies of the frontier molecular orbitals, which, in turn, govern the Cu(II/I) reduction potential and the relative absorption intensities at 450 nm and 600 nm.</p> </div> <br>

Synthetic models for active sites of reduced blue copper proteins: minimal geometric change between two oxidation states for fast self-exchange rate constants

2004 ◽  
Vol 7 (11) ◽  
pp. 1188-1190 ◽  
Author(s):  
Kiyoshi Fujisawa ◽  
Koyu Fujita ◽  
Tatsuya Takahashi ◽  
Nobumasa Kitajima ◽  
Yoshihiko Moro-oka ◽  
...  
Keyword(s):  
Exchange Rate ◽  
Rate Constants ◽  
Active Sites ◽  
Oxidation States ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Synthetic Models

scholarly journals The ‘methylamine oxidase’ system of an obligate methylotroph

1989 ◽  
Vol 260 (1) ◽  
pp. 75-79 ◽  
Author(s):  
K A Auton ◽  
C Anthony
Keyword(s):  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Optimum Growth ◽  
Methylamine Dehydrogenase ◽  
Obligate Methylotroph ◽  
Blue Copper ◽  
Oxidase System ◽  
High Copper

The terminal respiratory oxidase was solubilized from membranes of organism 4025, an obligate methylotroph. The partially purified oxidase is probably a cytochrome co. It does not oxidize amicyanin, but it oxidizes ‘azurin’ and cytochromes cH and cL. By using a complete ‘methylamine oxidase’ system reconstituted from pure methylamine dehydrogenase, purified oxidase and soluble blue copper proteins and cytochromes, it was confirmed that amicyanin is essential for methylamine oxidation; it could not be replaced by ‘azurin’ or cytochrome cH or cL. It was shown that the usual mediator between amicyanin and the oxidase is cytochrome cH, with ‘azurin’ able to replace it during growth at the high copper concentrations required for optimum growth of this unusual methylotroph.

Spectral and redox models for blue copper proteins: copper(II) complexes of β-diketonimines from a Knoevenagel condensate

1998 ◽  
Vol 72 (3-4) ◽  
pp. 101-107 ◽  
Author(s):  
K. Jeyasubramanian ◽  
S. Thambidurai ◽  
S.K. Ramalingam ◽  
R. Murugesan
Keyword(s):  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper
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