Theoretical analysis of resonance Raman spectra from the blue copper protein azurin

1990 ◽  
Vol 94 (5) ◽  
pp. 2160-2166 ◽  
Author(s):  
Mahfoud. Belhadj ◽  
John M. Jean ◽  
Richard A. Friesner ◽  
John. Schoonover ◽  
William H. Woodruff
Keyword(s):  
Theoretical Analysis ◽  
Raman Spectra ◽  
Resonance Raman ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Resonance Raman Spectra

ChemInform Abstract: RESONANCE RAMAN SPECTRA OF COPPER-SULFUR COMPLEXES AND THE BLUE COPPER PROTEIN QUESTION

1978 ◽  
Vol 9 (49) ◽  
Author(s):  
N. S. FERRIS ◽  
W. H. WOODRUFF ◽  
D. B. RORABACHER ◽  
T. E. JONES ◽  
L. A. OCHRYMOWYCZ
Keyword(s):  
Raman Spectra ◽  
Resonance Raman ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Resonance Raman Spectra

Resonance Raman spectra of copper-sulfur complexes and the blue copper protein question

1978 ◽  
Vol 100 (18) ◽  
pp. 5939-5942 ◽  
Author(s):  
Nancy S. Ferris ◽  
William H. Woodruff ◽  
David B. Rorabacher ◽  
T. E. Jones ◽  
L. A. Ochrymowycz
Keyword(s):  
Raman Spectra ◽  
Resonance Raman ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Resonance Raman Spectra

Resonance Raman spectra of cucumber basic blue copper protein ‘plantacyanin’

1986 ◽  
Vol 123 (4) ◽  
pp. L21-L22 ◽  
Author(s):  
Takeshi Sakurai ◽  
Satoshi Sawada ◽  
Akitsugu Nakahara
Keyword(s):  
Raman Spectra ◽  
Resonance Raman ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
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.

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