Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Peroxidases have conquered a prominent position in biotechnology and associated
research areas (enzymology, biochemistry, medicine, genetics, physiology, histo-and …

Scientists in such fields as mathematics, physics, chemistry, biochemistry, biology, and
medicine are currently involved in investigations of porphyrins and their numerous …

Publisher Summary Malaria is one of the most deadly infectious diseases known to
mankind. The species of Plasmodium that cause malaria can develop resistance to …

Although it is generally accepted that the tripeptide 6-(L-«-aminoadipoyl)-L-cysteinyl-D-
valine (lld-ACV)(1) is the direct precursor to isopenicillin N (2), 1, 2 the in-timate details of …

Heme proteins are a class of biologically important macromolecules that have a unique,
common active site: an ironrprotoporphyrin-IX complex shown in Figure 1. This “heme” unit …

Extended X-ray absorption fine structure spectroscopy has been utilized to determine the
structural environment of the heme iron sites in horseradish peroxidase compounds I and II …

Ferrylhemoglobin (X-FeIV-OH, where X denotes an amino acid residue in the globin moiety)
has long been suspected as a cytotoxic agent produced by the interaction of oxyhemoglobin …

The reaction between unligated (tetramesitylporphyrin) iron (II)(TMPFe11) and dioxygen in a
toluene solution has been examined by NMR spectroscopy. At-70 C, TMPFe11 reacts with …

Sperm whale metmyoglobin, which has tyrosine residues at positions 103, 146, and 151,
dimerizes in the presence of H2O2. Equine metmyoglobin, which lacks Tyr-151, and red …