Microbial cytochromes c' contain a 5-coordinate His-ligated heme that forms
stable adducts with nitric oxide (NO) and carbon monoxide (CO), but not wi
th dioxygen, We report the 1.95 and 1.35 Angstrom resolution crystal struct
ures of the CO- and NO-bound forms of the reduced protein from Alcaligenes
xylosoxidans, NO disrupts the His-Fe bond and binds in a novel mode to the
proximal face of the heme, giving a 5-coordinate species. In contrast, CO b
inds 6-coordinate on the distal side. A second CO molecule, not bound to th
e heme, is located in the proximal pocket. Since the unusual spectroscopic
properties of cytochromes c' are shared by soluble guanylate cyclase (sGC),
our findings have potential implications for the activation of sGC induced
by the binding of NO or CO to the heme domain.