Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding

1981 ◽  
Vol 671 (2) ◽  
pp. 177-183 ◽  
Author(s):  
A. Desbois ◽  
M. Lutz ◽  
R. Banerjee
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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