scholarly journals Soluble Guanylate Cyclase Is Activated Differently by Excess NO and by YC-1: Resonance Raman Spectroscopic Evidence

Biochemistry ◽  
2010 ◽  
Vol 49 (23) ◽  
pp. 4864-4871 ◽  
Author(s):  
Mohammed Ibrahim ◽  
Emily R. Derbyshire ◽  
Alexandra V. Soldatova ◽  
Michael A. Marletta ◽  
Thomas G. Spiro
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic

Resonance Raman spectroscopic evidence for a common [3-iron-4-sulfur] structure among proteins containing three-iron centers

1983 ◽  
Vol 105 (22) ◽  
pp. 6671-6678 ◽  
Author(s):  
Michael K. Johnson ◽  
Roman S. Czernuszewicz ◽  
Thomas G. Spiro ◽  
James A. Fee ◽  
William V. Sweeney
Keyword(s):  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic

Resonance Raman Evidence for the Presence of Two Heme Pocket Conformations with Varied Activities in CO-Bound Bovine Soluble Guanylate Cyclase and Their Conversion

Biochemistry ◽  
2005 ◽  
Vol 44 (3) ◽  
pp. 939-946 ◽  
Author(s):  
Zhengqiang Li ◽  
Biswajit Pal ◽  
Shigeo Takenaka ◽  
Shingo Tsuyama ◽  
Teizo Kitagawa
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman ◽  
Heme Pocket

Entry of water into the distal heme pocket of soluble guanylate cyclase β1 H-NOX domain alters the ligated CO structure: a resonance Raman and in silico simulation study

RSC Advances ◽  
2016 ◽  
Vol 6 (49) ◽  
pp. 43707-43714
Author(s):  
Haoran Xu ◽  
Yuebin Zhang ◽  
Lei Chen ◽  
Yan Li ◽  
Chen Li ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Simulation Study ◽  
In Silico ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman ◽  
Heme Pocket ◽  
In Silico Simulation

Water accessing into the heme pocket and alters the structures of CO–sGC (heme), exhibiting two different vFe–CO stretching modes.

Electronic and resonance raman spectroscopic evidence for identification of μ-trihalobis(triammine-ruthenium)(2+) ions as delocalized Ru(II,III) mixed-valence complexes

1984 ◽  
Vol 89 (3) ◽  
pp. L33-L34 ◽  
Author(s):  
Robert S. Armstrong ◽  
James K. Beattie ◽  
Patricia Del Favero ◽  
Vivienne M. Ellis ◽  
Noel S. Hush
Keyword(s):  
Mixed Valence ◽  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic

Structural characterization of nitric oxide-bound soluble Guanylate Cyclase using resonance Raman spectroscopy

2013 ◽  
Vol 17 (03) ◽  
pp. 240-246
Author(s):  
Biswajit Pal ◽  
Katsuhiro Tanaka ◽  
Shigeo Takenaka ◽  
Tajith B. Shaik ◽  
Teizo Kitagawa
Keyword(s):  
Nitric Oxide ◽  
Raman Spectroscopy ◽  
Guanylate Cyclase ◽  
Protein Interactions ◽  
Bound States ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Bending Modes

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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