Biochemistry · 2011 · 56 citations · 24 references
Life SciencesBiochemistryPharmacologyEnzymologyMetabolic StabilityRedox BiochemistryHeme Redox ChemistryRedox SignalingFerric Heme ReactivityFerrous Heme ReactivityGlutathione Redox SystemGuanylyl Cyclase IsoformsMyoglobin OxidationNitric OxideNitric Oxide Binding To HemeOxidant Chemistry
Oxidation and loss of heme in soluble guanylyl/guanylate cyclase (sGC), the nitric oxide receptor, is thought to be a major contributor to cardiovascular disease and is the target of compounds BAY 58-2667 and HMR1766. Using spectroelectrochemical titration, we found a truncated sGC to be highly stable in the ferrous state (234 mV) and to bind ferrous heme tightly even in the presence of NO, despite the NO-induced release of the proximal histidine. In contrast, oxidized sGC readily loses ferric heme to myoglobin (0.47 ± 0.02 h(-1)). Peroxynitrite, the presumed cellular oxidant, readily oxidizes sGC in 5 mM glutathione.
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Femtomolar Sensitivity of a NO Sensor from <i>Clostridium botulinum</i>
P. Nioche, Vladimír Berka, Julia Vipond et al. · Science · 2004 · 188 citations