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Structural comparison of FeII and FeII-NO structures. Overlay of FeII (wheat) and FeII-NO (red) (molecules A of the ASU) crystal structures following alignment of the proximal subdomains (residues 95–180) showing displacement of the distal subdomain upon NO binding and breakage of the iron–histidine bond. Conserved glycines (G70 and G144, highlighted in green) in helices αD and αG serve as a hinge point for subdomain rotation within So H-NOX.
