Determination of the Magnetic Axes of Cobalt(II) and Nickel(II) Azurins from1H NMR Data:  Influence of the Metal and Axial Ligands on the Origin of Magnetic Anisotropy in Blue Copper Proteins†

Biochemistry ◽  
1998 ◽  
Vol 37 (24) ◽  
pp. 8659-8673 ◽  
Author(s):  
Antonio Donaire ◽  
Jesús Salgado ◽  
José-María Moratal
Keyword(s):  
Magnetic Anisotropy ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Axial Ligands ◽  
Nmr Data

Determination of the Self-Exchange Rate Constant for Rusticyanin from Thiobacillus ferrooxidans and a Comparison with Values for Other Type 1 Blue Copper Proteins

1995 ◽  
Vol 34 (21) ◽  
pp. 5370-5374 ◽  
Author(s):  
Panayotis Kyritsis ◽  
Christopher Dennison ◽  
W. John Ingledew ◽  
William McFarlane ◽  
A. Geoffrey Sykes
Keyword(s):  
Exchange Rate ◽  
Rate Constant ◽  
Thiobacillus Ferrooxidans ◽  
The Self ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Exchange Rate Constant

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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