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 6th edition of this classic comprises the most comprehensive guide to infrared and
Raman spectra of inorganic, organometallic, bioinorganic, and coordination compounds …

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 …

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

0009-2665/94/0794-0659 $14.00/0 fascination for molecular scientists. Our present un-
derstanding of how hemoglobin works has arisen from a notable interplay of studies on both …

An axiom of hemoprotein biochemistry is that mo-lecular structure provides the basis for an
understand-ing of how these proteins work. Chemical curiosity is aroused by the …

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 …

Metalloporphyrins are exceedingly useful building blocks for the design and synthesis of
molecularly based solids. The use of hydrogen bonding or metal ion coordination provides a …

Hemoglobin (Hb) is the respiratory protein of the red blood cells which carries 02 from the
lungs to the tissues and facilitates the return transport of C02 from the tissues to the lungs …