ArticleBiochemistry2012
Conformationally distinct five-coordinate heme-NO complexes of soluble guanylate cyclase elucidated by multifrequency electron paramagnetic resonance (EPR).
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Roles of Three Conserved Active Site Residues of CytochromeJournal of the American Chemical Society · 2025Article
- Nitric oxide signaling in ctenophores.Frontiers in neuroscience · 2023Article
- The diversification and lineage-specific expansion of nitric oxide signaling in Placozoa: insights in the evolution of gaseous transmission.Scientific reports · 2020Article
- Regulation of nitric oxide signaling by formation of a distal receptor-ligand complex.Nature chemical biology · 2017Article
- The selectivity of Vibrio cholerae H-NOX for gaseous ligands follows the "sliding scale rule" hypothesis. Ligand interactions with both ferrous and ferric Vc H-NOX.Biochemistry · 2013Article
- EPR characterisation of the ferrous nitrosyl complex formed within the oxygenase domain of NO synthase.Chembiochem : a European journal of chemical biology · 2013Article
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Authors and funding
4 authors.
Funding
Abstract
Soluble guanylate cyclase (sGC) is a heme-containing enzyme that senses nitric oxide (NO). Formation of a heme Fe-NO complex is essential to sGC activation, and several spectroscopic techniques, including electron paramagnetic resonance (EPR) spectroscopy, have been aimed at elucidating the active enzyme conformation. Of these, only EPR spectra (X-band ~9.6 GHz) have shown differences between low- and high-activity Fe-NO states, and these states are modeled in two different heme domain truncations of sGC, β1(1-194) and β2(1-217), respectively (Derbyshire et al., Biochemistry 2008, 47, 3892-3899). The EPR signal of the low-activity sGC Fe-NO complex exhibits a broad lineshape that has been interpreted as resulting from site-to-site inhomogeneity, and simulated using g strain, a continuous distribution about the principal values of a given g tensor. This approach, however, fails to account for visible features in the X-band EPR spectra as well as the g anisotropy observed at higher microwave frequencies. Herein we analyze X-, Q-, and D-band EPR spectra and show that both the broad lineshape and the spectral structure of the sGC EPR signal at multiple microwave frequencies can be simulated successfully with a superposition of only two distinct g tensors. These tensors represent different populations that likely differ in Fe-NO bond angle, hydrogen bonding, or the geometry of the amino acid residues. One of these conformations can be linked to a form of the enzyme with higher activity.
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