A Comparison of the Inner-Sphere Reorganization Energies of Cytochromes, Iron−Sulfur Clusters, and Blue Copper Proteins

2001 ◽  
Vol 105 (23) ◽  
pp. 5546-5552 ◽  
Author(s):  
Emma Sigfridsson ◽  
Mats H. M. Olsson ◽  
Ulf Ryde
Keyword(s):  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Iron Sulfur Clusters ◽  
Blue Copper ◽  
Iron Sulfur ◽  
Inner Sphere ◽  
Reorganization Energies

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

Structure and Electron Transfer Reactions of Blue Copper Proteins

1977 ◽  
pp. 145-155 ◽  
Author(s):  
HARRY B. GRAY ◽  
CATHERINE L. COYLE ◽  
DAVID M. DOOLEY ◽  
PAULA J. GRUNTHANER ◽  
JEFFREY W. HARE ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Transfer Reactions ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Electron Transfer Reactions

ChemInform Abstract: RESONANCE RAMAN STUDIES OF ′BLUE′ COPPER PROTEINS

1974 ◽  
Vol 5 (44) ◽  
pp. no-no
Author(s):  
OLAVI SIIMAN ◽  
N. MARTIN YOUNG ◽  
PAUL R. CAREY
Keyword(s):  
Resonance Raman ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper
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