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.

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

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.

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

scholarly journals The emergence of DNA in the RNA world: an in silico simulation study of genetic takeover

2015 ◽  
Vol 15 (1) ◽  
Author(s):  
Wentao Ma ◽  
Chunwu Yu ◽  
Wentao Zhang ◽  
Sanmao Wu ◽  
Yu Feng
Keyword(s):  
Simulation Study ◽  
In Silico ◽  
Rna World ◽  
In Silico Simulation ◽  
Genetic Takeover

scholarly journals Evaluation of a novel closed-loop fluid-administration system based on dynamic predictors of fluid responsiveness: an in silico simulation study

Critical Care ◽  
2011 ◽  
Vol 15 (6) ◽  
pp. R278 ◽  
Author(s):  
Joseph Rinehart ◽  
Brenton Alexander ◽  
Yannick Manach ◽  
Christoph Hofer ◽  
Benoit Tavernier ◽  
...  
Keyword(s):  
Fluid Responsiveness ◽  
Simulation Study ◽  
In Silico ◽  
Closed Loop ◽  
Fluid Administration ◽  
Administration System ◽  
In Silico Simulation

Interaction of Soluble Guanylate Cyclase with YC-1:  Kinetic and Resonance Raman Studies†

Biochemistry ◽  
2000 ◽  
Vol 39 (14) ◽  
pp. 4191-4198 ◽  
Author(s):  
John W. Denninger ◽  
Johannes P. M. Schelvis ◽  
Philip E. Brandish ◽  
Yunde Zhao ◽  
Gerald T. Babcock ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman
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