Significance: Ligand selectivity for dioxygen (O2), carbon monoxide (CO), and nitric oxide
(NO) is critical for signal transduction and is tailored specifically for each heme-protein …

Physiological bond formation and bond breaking events between proteins and ligands and
their immediate consequences are difficult to synchronize and study in general. However …

Selectivity among NO, CO, and O2 is crucial for the physiological function of most heme
proteins. Although there is a million-fold variation in equilibrium dissociation constants (KD) …

Some classes of bacteria within phyla possess protein sensors identified as homologous to
the heme domain of soluble guanylate cyclase, the mammalian NO-receptor. Named H-NOX …

In the decade since the discovery of androglobin, a multi-domain hemoglobin of metazoans
associated with ciliogenesis and spermatogenesis, there has been little advance in the …

Soluble guanylyl cyclase (sGC), the key enzyme for the formation of second messenger
cyclic GMP, is an authentic sensor for nitric oxide (NO). Binding of NO to sGC leads to strong …

The structural basis by which gas-binding heme proteins control their interactions with NO,
CO, and O 2 is fundamental to enzymology, biotechnology, and human health. Cytochromes …

We have determined the 1.8 Å X-ray crystal structure of a monoheme c-type cytochrome,
cytochrome P460, from Nitrosomonas europea. The chromophore possesses unusual …

A wide and still rapidly increasing range of heme-based sensor proteins has been
discovered over the last two decades. At the molecular level, these proteins function as …

We investigated the ultrafast structural transitions of the heme induced by nitric oxide (NO)
binding for several heme proteins by subpicosecond time-resolved resonance Raman and …