The metallobiochemistry underlying the formation of the inorganic N–N-bond-containing
molecules nitrous oxide (N2O), dinitrogen (N2), and hydrazine (N2H4) is essential to the …

Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical
nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas and water …

Allosteric heme proteins can fulfill a very large number of different functions thanks to the
remarkable chemical versatility of heme through the entire living kingdom. Their efficacy …

The A51V variant of human cytochrome c is linked to thrombocytopenia 4 (THC4), a
condition that causes decreased blood platelet counts. A 1.82 Å structure of the A51V variant …

Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide. They
bear specialized “heme P460” cofactors that are cross-linked to their host polypeptides by a …

Cytochrome c binds to cardiolipin (CL) on the inner mitochondrial membrane during the
initial stages of apoptosis where it oxidizes CL, promoting its release into the cytoplasm …

Lys-ligated cytochromes make up an emerging family of heme proteins. Density functional
theory calculations on the amine/imidazole-ligated c-type ferric heme were employed to …

Ligand substitution at the metal center is common in catalysis and signal transduction of
metalloproteins. Understanding the effects of particular ligands, as well as the polypeptide …

The hydroxylamine oxidoreductase/hydrazine dehydrogenase (HAO/HDH) protein family
constitutes an important group of octaheme cytochromes c (OCCs). The majority of these …

Oxidation of cardiolipin (CL) by cytochrome c (cyt c) has been proposed to initiate the
intrinsic pathway of apoptosis. Domain-swapped dimer (DSD) conformations of cyt c have …