Structural Characterization of the Catalytic High-Spin Hemebof Nitric Oxide Reductase:  A Resonance Raman Study†

1998 ◽  
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Pierre Moënne-Loccoz ◽  
Simon de Vries

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Takehiko Tosha ◽  
Nozomi Sato ◽  
Norihiro Okada ◽  
Hiroshi Sugimoto ◽  
Yoshitsugu Shiro


1991 ◽  
Vol 1059 (1) ◽  
pp. 37-44 ◽  
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J. David Hobbs ◽  
Max Wynn ◽  
David J. Nunez ◽  
Richard Malkin ◽  
David B. Knaff ◽  
...  


2010 ◽  
Vol 49 (16) ◽  
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Ismail Hijazi ◽  
Thierry Roisnel ◽  
Pascale Even-Hernandez ◽  
Florence Geneste ◽  
Olivier Cador ◽  
...  


2006 ◽  
Vol 45 (14) ◽  
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Habib Nasri ◽  
Mary K. Ellison ◽  
Ben Shaevitz ◽  
Govind P. Gupta ◽  
W. Robert Scheidt


Author(s):  
João B. Vicente ◽  
Francesca M. Scandurra ◽  
Elena Forte ◽  
Maurizio Brunori ◽  
Paolo Sarti ◽  
...  




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Vol 17 (03) ◽  
pp. 240-246
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Biswajit Pal ◽  
Katsuhiro Tanaka ◽  
Shigeo Takenaka ◽  
Tajith B. Shaik ◽  
Teizo Kitagawa

Mammalian soluble Guanylate Cyclase (sGC), working as a physiological NO receptor, is investigated using resonance Raman spectroscopy for NO bound states with different saturation levels in the presence and absence of effectors. The Fe–NO (νFe–NO) and N–O (νN-O) stretching bands appeared at 521 and 1681 cm-1, respectively, without effectors, but νN-O was split into 1681 and 1699 cm-1 in the presence of GTP and shifted to 1687 cm-1 in the presence of YC-1 or BAY 41-2272, while νFe-NO remained unaltered. The split two νN-O bands were independent of NO saturation levels. GTP or YC-1/BAY 41-2272 altered the vinyl and propionate bending modes from 423 to 399 cm-1 and 376 to 367 cm-1, respectively. Based on these observations, allosteric effects on NO …protein interactions are discussed.



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