Heme sensor proteins are present in organisms ranging from bacteria to mammals, typically
consisting of a catalytic domain and a heme‐containing sensor domain, which can bind …

A recently proposed pathway for heme b biosynthesis, common to diverse bacteria, has the
conversion of two of the four propionates on coproheme III to vinyl groups as its final step …

X-ray induced radiation damage of protein crystals is well known to occur even at cryogenic
temperatures. Redox active sites like metal sites seem especially vulnerable for these …

Coproheme decarboxylases (ChdCs) are utilized by monoderm bacteria to produce heme b
by a stepwise oxidative decarboxylation of the 2-and 4-propionate groups of iron …

In heme proteins, the canonical and reversed conformations result from the rotation of the
heme group by 180° about the α, γ‐meso axis in the protein pocket. The coexistence of the …

Bifunctional enzymes, which contain two domains with opposing enzymatic activities, are
widely distributed in bacteria, but the regulatory mechanism (s) that prevent futile cycling are …

Heme-based sensor proteins are used by organisms to control signaling and physiological
effects in response to their gaseous environment. Globin-coupled sensors (GCS) are oxygen …

Inspection of heme protein structures in the protein data bank reveals four isomers of heme
characterized by different relative orientations of the vinyl side chains; remarkably, all these …

Resonance Raman spectroscopy is employed to characterize heme site structural changes
arising from conformational heterogeneity in deoxyMb and ligated derivatives, ie, the ferrous …

Resonance Raman spectra are reported for substrate-free and camphor-bound cytochrome
P450cam and its isotopically labeled analogues that have been reconstituted with …