Expression and Characterization of the Catalytic Domains of Soluble Guanylate Cyclase:  Interaction with the Heme Domain†

Biochemistry ◽  
2005 ◽  
Vol 44 (10) ◽  
pp. 4083-4090 ◽  
Author(s):  
Jonathan A. Winger ◽  
Michael A. Marletta
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Catalytic Domains ◽  
Heme Domain

Resonance Raman Characterization of the Heme Domain of Soluble Guanylate Cyclase†

Biochemistry ◽  
1998 ◽  
Vol 37 (46) ◽  
pp. 16289-16297 ◽  
Author(s):  
Johannes P. M. Schelvis ◽  
Yunde Zhao ◽  
Michael A. Marletta ◽  
Gerald T. Babcock
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman ◽  
Heme Domain ◽  
Raman Characterization

Characterization of a Carbon Monoxide-Activated Soluble Guanylate Cyclase fromChlamydomonas reinhardtii

Biochemistry ◽  
2019 ◽  
Vol 58 (17) ◽  
pp. 2250-2259 ◽  
Author(s):  
Benjamin G. Horst ◽  
Edna M. Stewart ◽  
Aren A. Nazarian ◽  
Michael A. Marletta
Keyword(s):  
Carbon Monoxide ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase

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 Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Benjamin G Horst ◽  
Adam L Yokom ◽  
Daniel J Rosenberg ◽  
Kyle L Morris ◽  
Michal Hammel ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Electron Microscopy ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Coiled Coil ◽  
X Ray ◽  
Nitric Oxide Signaling ◽  
Catalytic Domains ◽  
X Ray Scattering ◽  
Cryo Electron Microscopy

Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO) in mammalian nitric oxide signaling. We determined structures of full-length Manduca sexta sGC in both inactive and active states using cryo-electron microscopy. NO and the sGC-specific stimulator YC-1 induce a 71° rotation of the heme-binding β H-NOX and PAS domains. Repositioning of the β H-NOX domain leads to a straightening of the coiled-coil domains, which, in turn, use the motion to move the catalytic domains into an active conformation. YC-1 binds directly between the β H-NOX domain and the two CC domains. The structural elongation of the particle observed in cryo-EM was corroborated in solution using small angle X-ray scattering (SAXS). These structures delineate the endpoints of the allosteric transition responsible for the major cyclic GMP-dependent physiological effects of NO.

scholarly journals Characterization of Two Different Five-Coordinate Soluble Guanylate Cyclase Ferrous–Nitrosyl Complexes†

Biochemistry ◽  
2008 ◽  
Vol 47 (12) ◽  
pp. 3892-3899 ◽  
Author(s):  
Emily R. Derbyshire ◽  
Alexander Gunn ◽  
Mohammed Ibrahim ◽  
Thomas G. Spiro ◽  
R. David Britt ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Nitrosyl Complexes

Generation and Characterization of a Stable Soluble Guanylate Cyclase-Overexpressing CHO Cell Line

Nitric Oxide ◽  
1999 ◽  
Vol 3 (1) ◽  
pp. 55-66 ◽  
Author(s):  
Eva Maria Becker ◽  
Frank Wunder ◽  
Raimund Kast ◽  
Chantal Robyr ◽  
Markus Hoenicka ◽  
...  
Keyword(s):  
Cell Line ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Cho Cell ◽  
Cho Cell Line
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