YC-1 Binding to the β Subunit of Soluble Guanylyl Cyclase Overcomes Allosteric Inhibition by the α Subunit

Purohit, Rahul; Fritz, Bradley G.; The, Juliana; Issaian, Aaron; Weichsel, Andrzej; David, Cynthia L.; Campbell, Eric; Hausrath, Andrew C.; Rassouli-Taylor, Leida; Garcin, Elsa D.; Gage, Matthew J.; Montfort, William R.

doi:10.1021/bi4015133

Cited by 35Hemoglobin structure and functionNitric Oxide and Endothelin EffectsReceptor Mechanisms and Signaling

YC-1 Binding to the β Subunit of Soluble Guanylyl Cyclase Overcomes Allosteric Inhibition by the α Subunit

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Purohit, Rahul, Fritz, Bradley G., The, Juliana, Issaian, Aaron, Weichsel, Andrzej, David, Cynthia L., Campbell, Eric, Hausrath, Andrew C. +4 more·2014·Biochemistry

DOI 10.1021/bi4015133PMC PMC3914721

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Abstract

Soluble guanylate cyclase (sGC) is a heterodimeric heme protein and the primary nitric oxide receptor. NO binding stimulates cyclase activity, leading to regulation of cardiovascular physiology and making sGC an attractive target for drug discovery. YC-1 and related compounds stimulate sGC both independently and synergistically with NO and CO binding; however, where the compounds bind and how they work remain unknown. Using linked equilibrium binding measurements, surface plasmon resonance, and domain truncations in Manduca sexta and bovine sGC, we demonstrate that YC-1 binds near or directly to the heme-containing domain of the β subunit. In the absence of CO, YC-1 binds with a Kd of 9-21 μM, depending on the construct. In the presence of CO, these values decrease to 0.6-1.1 μM. Pfizer compound 25 bound ∼10-fold weaker than YC-1 in the absence of CO, whereas compound BAY 41-2272 bound particularly tightly in the presence of CO (Kd = 30-90 nM). Additionally, we found that CO binds much more weakly to heterodimeric sGC proteins (Kd = 50-100 μM) than to the isolated heme domain (Kd = 0.2 μM for Manduca β H-NOX/PAS). YC-1 greatly enhanced binding of CO to heterodimeric sGC, as expected (Kd ∼ 1 μM). These data indicate the α subunit induces a heme pocket conformation with a lower affinity for CO and NO. YC-1 family compounds bind near the heme domain, overcoming the α subunit effect and inducing a heme pocket conformation with high affinity. We propose this high-affinity conformation is required for the full-length protein to achieve high catalytic activity.

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CYPOR, either directly or in combination with the CYP proteins, has been described as a source of superoxide.
“CYPOR, either directly or in combination with the CYP proteins, has been described as a source of superoxide (758, 851).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [758]

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Synthesis and characterization of NS-2028 analogues
Pyriochou, A., Giannis, A., & Papapetropoulos, A. (2009) · BMC Pharmacology · doi:10.1186/1471-2210-9-s1-p55
Increased ventilatory lung stretch alters the effect of soluble guanylyl cyclase-derived cGMP on endothelial barrier function in isolated mouse lungs
Schmidt, E., Gonzales, A., Servinsky, L., et al. (2007) · BMC Pharmacology · doi:10.1186/1471-2210-7-s1-p51

Authors: Purohit, R., Fritz, B. G., The, J., Issaian, A., Weichsel, A., David, C. L., Campbell, E., Hausrath, A. C., Rassouli-Taylor, L., Garcin, E. D., Gage, M. J., & Montfort, W. R.
Affiliations: University of Arizona (US)
Northern Arizona University (US)
University of Maryland, Baltimore County (US)
Corresponding author: Montfort, William R.
ORCID: Purohit, Rahul
Fritz, Bradley G.
Issaian, Aaron
Campbell, Eric
Garcin, Elsa D.
Gage, Matthew J.
Montfort, William R.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2013-12-30
Volume: 53
Issue: 1
Pages: 101-114
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi4015133
PMC: PMC3914721
OpenAlex: W2057106948
Cited by: 35
References: 77
Citations by year: 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 7 · 2017: 5 · 2016: 5 · 2015: 2 · 2014: 6
FWCI: 2.52
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (CA143924, HL062969)
American Heart Association (10SDG2600345, 11PRE7610113)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: soluble guanylate cyclase, YC-1, beta subunit, nitric oxide receptors, carbon monoxide binding, heme domain, BAY 41-2272, Manduca sexta, heterodimeric protein
MeSH terms: Soluble Guanylyl Cyclase, Allosteric Regulation, Animals, Carbon Monoxide, Cattle, Guanylate Cyclase, Heme, Indazoles, Models, Molecular, Nitric Oxide, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Receptors, Cytoplasmic and Nuclear, Manduca, Surface Plasmon Resonance, Protein Subunits

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YC-1 Binding to the β Subunit of Soluble Guanylyl Cyclase Overcomes Allosteric Inhibition by the α Subunit

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