Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …

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

The majority of modern organisms, including many prokaryotes, are aerobes; 1 that is, they
use molecular oxygen as the terminal electron acceptor for energy generation. Although …

AUosteric proteins control and coordinate chemical events in the living cell. When Monod
conceived that idea he said that he had discovered the second secret of life. The first was …

The structural elements which afford molecular recognition and discrimination events in
macromol-ecule-ligand interactions dictate the basis of protein function. Nature has evolved …

The two-volume Encyclopedia of Supramolecular Chemistry offers authoritative, centralized
information on a rapidly expanding interdisciplinary field. User-friendly and high-quality …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Time courses for the autooxidation of native and mutant sperm whale and pig myoglobins
were measured at 37 degrees C in the presence of catalase and superoxide dismutase. In …

The structure of human oxyhaemoglobin was determined by single crystal X-ray analysis at
2· 1resolution. Data were collected on an Arndt-Wonacott camera at− 2° C. The structure …

We have used x-ray crystallography to determine the structures of sperm whale myoglobin
(Mb) in four different ligation states (unligated, ferric aquomet, oxygenated, and …