Resonance Raman spectra of blue copper proteins: assignments from normal mode calculations and copper-63/copper-65 and H2O/D2O shifts for stellacyanin and laccase

Biochemistry ◽  
1984 ◽  
Vol 23 (6) ◽  
pp. 1084-1093 ◽  
Author(s):  
Lisa Nestor ◽  
James A. Larrabee ◽  
Geoffrey Woolery ◽  
Bengt Reinhammar ◽  
Thomas G. Spiro
Keyword(s):  
Raman Spectra ◽  
Normal Mode ◽  
Resonance Raman ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Normal Mode Calculations ◽  
Resonance Raman Spectra

Copper coordination group in blue copper proteins. Evidence from resonance Raman spectra

Biochemistry ◽  
1975 ◽  
Vol 14 (6) ◽  
pp. 1244-1250 ◽  
Author(s):  
V. Miskowski ◽  
S. P. W. Tang ◽  
T. G. Spiro ◽  
E. Shapiro ◽  
T. H. Moss
Keyword(s):  
Raman Spectra ◽  
Resonance Raman ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Copper Coordination ◽  
Resonance Raman Spectra

Resonance Raman spectra of plastocyanin and pseudoazurin: evidence for conserved cysteine ligand conformations in cupredoxins (blue copper proteins)

Biochemistry ◽  
1991 ◽  
Vol 30 (45) ◽  
pp. 10904-10913 ◽  
Author(s):  
Jane Han ◽  
Elinor T. Adman ◽  
Teruhiko Beppu ◽  
Rachel Codd ◽  
Hans C. Freeman ◽  
...  
Keyword(s):  
Raman Spectra ◽  
Resonance Raman ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Resonance Raman Spectra

scholarly journals Low-temperature resonance-Raman spectra of Japanese-lacquer-tree (Rhus vernicifera) laccase, type-2-copper-depleted laccase and H2O2-treated type-2-copper-depleted laccase

1983 ◽  
Vol 213 (2) ◽  
pp. 503-506 ◽  
Author(s):  
G Musci ◽  
A Desideri ◽  
L Morpurgo ◽  
A Garnier-Suillerot ◽  
L Tosi
Keyword(s):  
Raman Spectra ◽  
Strong Dependence ◽  
Resonance Raman ◽  
Local Symmetry ◽  
Structural Rearrangements ◽  
Blue Copper ◽  
Copper Site ◽  
Resonance Raman Spectra ◽  
Rhus Vernicifera

Resonance-Raman spectra of Japanese-lacquer-tree (Rhus vernicifera) laccase, type-2-copper-depleted laccase and the latter form treated with H2O2 were measured in liquid and frozen solution, on excitation into the 600 nm absorption band. Significant changes in intensity and/or frequency of the bands lying in the 370-430 cm-1 region were observed on freezing, indicating local structural rearrangements taking place at the blue copper site. These findings corroborate previous suggestions based on e.p.r. measurements and redox data [Morpurgo, Calabrese, Desideri & Rotilio (1981) Biochem. J. 193, 639-642]. They show the strong dependence of the physical properties of blue copper centres on local symmetry. Some conclusions on the origin of the Raman bands are also drawn.

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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