Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analog

Biochemistry ◽  
1983 ◽  
Vol 22 (13) ◽  
pp. 3202-3206 ◽  
Author(s):  
Wolfgang Maret ◽  
Michael Zeppezauer ◽  
Joann Sanders-Loehr ◽  
Thomas M. Loehr
1998 ◽  
Vol 120 (49) ◽  
pp. 12791-12797 ◽  
Author(s):  
Di Qiu ◽  
Siddharth Dasgupta ◽  
Pawel M. Kozlowski ◽  
William A. Goddard ◽  
Thomas G. Spiro

1983 ◽  
Vol 213 (2) ◽  
pp. 503-506 ◽  
Author(s):  
G Musci ◽  
A Desideri ◽  
L Morpurgo ◽  
A Garnier-Suillerot ◽  
L Tosi

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.


2010 ◽  
Vol 83 (10) ◽  
pp. 1162-1169
Author(s):  
Tomoko Miyazaki ◽  
Chizu Shimokawa ◽  
Toshio Matsushita ◽  
Shinobu Itoh ◽  
Junji Teraoka

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