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

Vc H-NOX (or VCA0720) is an H-NOX (heme-nitric oxide and oxygen binding) protein from facultative aerobic bacterium Vibrio cholerae. It shares significant sequence homology with soluble guanylyl cyclase (sGC), a NO sensor protein commonly found in animals. Similar to sGC, Vc H-NOX binds strongly to NO and CO with affinities of 0.27 nM and 0.77 μM, respectively, but weakly to O2. When positioned on a “sliding scale” plot [Tsai, A.-l., et al. (2012) Biochemistry 51, 172–186], the line connecting log KD(NO) and log KD(CO) of Vc H-NOX can almost be superimposed with that of Ns H-NOX. Therefore, the measured affinities and kinetic parameters of gaseous ligands to Vc H-NOX provide more evidence to validate the “sliding scale rule” hypothesis. Like sGC, Vc H-NOX binds NO in multiple steps, forming first a six-coordinate heme–NO complex at a rate of 1.1 × 109 M–1 s–1, and then converts to a five-coordinate heme–NO complex at a rate that is also dependent on NO concentration. Although the formation of oxyferrous V...