Cytochromes P450 constitute a broad class of heme monooxygenase enzymes with more
than 11,500 isozymes which have been identified in organisms from all biological kingdoms …

Carbon monoxide is a useful vibrational probe of heme binding sites in proteins, because
FeCO backbonding is modulated by polar interactions with protein residues, and by …

The gaseous XO molecules (X= C, N or O) bind to the heme prosthetic group of heme
proteins, and thereby activate or inhibit key biological processes. These events depend on …

Creating artificial protein families affords new opportunities to explore the determinants of
structure and biological function free from many of the constraints of natural selection. We …

The mammalian transcription factor Bach1 functions as a repressor of the enhancers of
heme oxygenase‐1 (HO‐1) gene (Hmox‐1) by forming heterodimers with the small Maf …

The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often
under physiological conditions, catalyze many distinct oxidative transformations on a wide …

Cytochrome P450cam was subjected to high pressures of 2.2 kbar, converting the enzyme
to its inactive form, P420cam. The resultant protein was characterized by electron …

A current question in nitric oxide (NO) biology is whether NO can act as a feedback inhibitor
of NO synthase (NOS). We have approached this problem by examining the interaction of …

Structural and functional roles of the hydrogen bonding network that surrounds the heme-
thiolate coordination of P450cam from Pseudomonas putida were investigated. A hydrogen …

Fungal nitric-oxide reductase (NOR) is a heme enzyme that catalyzes the reduction of NO to
N 2 O through its ferric-NO complex, the first intermediate of the catalysis. Crystal structures …