The electrochemistry of some copper-containing proteins and enzymes, viz. azurin,
galactose oxidase, tyrosinase (catechol oxidase), and the “blue” multicopper oxidases …

In this review we present a broad survey of fundamental scientific and medically applied
studies on keyhole limpet hemocyanin (KLH). Commencing with the biochemistry of KLH …

The enzymes tyrosinase, catecholoxidase and hemocyanin all share similar active sites,
although their physiological functions differ. Hemocyanins serve as oxygen carrier proteins …

Arthropod hemocyanins are large, multimeric,(n× 6) copper-containing proteins that deliver
oxygen in the haemolymph of many chelicerate, crustacean, myriapod, and also possibly …

An enzyme generally catalyzes one well defined reaction with high specificity and efficiency.
We report here in contrast that the copper protein hemocyanin of the tarantulaEurypelma …

The first line of defence of arthropods against pathogens and parasites is of physical nature
via their hard cuticle. However, once this barrier is passed, a complex interaction of innate …

Hemocyanin is an extracellular, blue protein that occurs in high concentrations in the blood
of many arthropods, including spiders, scorpions, horseshoe crabs, crustaceans, and at …

This review summarizes recent highlights of our joint work on the structure, evolution, and
function of a family of highly complex proteins, the hemocyanins. They are blue-pigmented …

Phenoloxidase, widely distributed among animals, plants, and fungi, is involved in many
biologically essential functions including sclerotization and host defense. In chelicerates, the …

How Does Tyrosinase Work? Recent Insights from Model Chemistry and Structural Biology
This work was supported by the Medicine and Science Center of the University of Mainz (HD) …