Fe2S2 protein resonance Raman spectra revisited: structural variations among adrenodoxin, ferredoxin, and red paramagnetic protein

1989 ◽  
Vol 111 (10) ◽  
pp. 3505-3511 ◽  
Author(s):  
Sanghwa Han ◽  
Roman S. Czernuszewicz ◽  
Tokuji Kimura ◽  
Michael W. W. Adams ◽  
Thomas G. Spiro



2008 ◽  
Author(s):  
X. K. Shen ◽  
H. Ling ◽  
Y. F. Lu






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


1978 ◽  
Vol 51 (9) ◽  
pp. 2735-2736 ◽  
Author(s):  
Masao Tahara ◽  
Susumu Matsuzaki ◽  
Shiro Maeda


2015 ◽  
Vol 72 ◽  
pp. 1-6 ◽  
Author(s):  
Shuo Li ◽  
Zhanlong Li ◽  
Shenghan Wang ◽  
Shuqin Gao ◽  
Chenglin Sun ◽  
...  




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