Nitric oxide (NO) is an important signaling molecule that is involved in a wide range of
physiological and pathological events in biology. Metal coordination chemistry, especially …

Conspectus Metal ions and metallocofactors play important roles in a broad range of
biochemical reactions. Accordingly, it has been estimated that as much as 25–50% of the …

At the onset of apoptosis, the peroxidation of cardiolipin at the inner mitochondrial
membrane by cytochrome c requires an open coordination site on the heme. We report a …

Heme is an essential and functionally versatile cofactor. Our understanding of how the
environment of a heme in a protein tunes its function has benefited from spectroscopic and …

Heme c is characterized by its covalent attachment to a polypeptide. The attachment is
typically to a CXXCH motif in which the two Cys form thioether bonds with the heme,“X” can …

Nitrophorins (NPs) catalyze the nitrite dismutation reaction that is unprecedented in
ferriheme proteins. Despite progress in studying the reaction mechanism, fundamental …

Analysis of NMR spectra reveals that the heme axial Met ligand orientation and dynamics in
Nitrosomonas europaea cytochrome c 552 (Ne cyt c) are dependent on the heme redox …

Approximately 40% of all proteins are metalloproteins, and approximately 80% of Earth's
ecosystems are at temperatures≤ 5° C, including 90% of the global ocean. Thus, an …

The exponential increase in protein structures deposited in the Protein Data Bank (PDB) has
resulted in the elucidation of most, if not all, protein folds, thus making molecular …

Heme c is characterized by its covalent attachment to a polypeptide. The attachment is
typically to a CXXCH motif in which the two Cys form thioether bonds with the heme,“X” can …