Copper active sites in biology

EI Solomon, DE Heppner, EM Johnston… - Chemical …, 2014 - ACS Publications
On the basis of its generally accessible I/II redox couple and bioavailability, copper plays a
wide variety of roles in nature that mostly involve electron transfer (ET), O 2 binding …

The prophenoloxidase‐activating system in invertebrates

L Cerenius, K Söderhäll - Immunological reviews, 2004 - Wiley Online Library
A major innate defense system in invertebrates is the melanization of pathogens and
damaged tissues. This important process is controlled by the enzyme phenoloxidase (PO) …

Plastic degradation by insect hexamerins: Near-atomic resolution structures of the polyethylene-degrading proteins from the wax worm saliva

M Spínola-Amilibia, R Illanes-Vicioso, E Ruiz-López… - Science …, 2023 - science.org
Plastic waste management is a pressing ecological, social, and economic challenge. The
saliva of the lepidopteran Galleria mellonella larvae is capable of oxidizing and …

Copper–O 2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme

M Rolff, J Schottenheim, H Decker… - Chemical Society Reviews, 2011 - pubs.rsc.org
The critical review describes the known dicopper systems mediating the aromatic
hydroxylation of monophenolic substrates. Such systems are of interest as structural and …

Activation of dioxygen by copper metalloproteins and insights from model complexes

DA Quist, DE Diaz, JJ Liu, KD Karlin - JBIC Journal of Biological Inorganic …, 2017 - Springer
Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the
enzymes that are utilized for these reactions are copper-containing metalloenzymes, which …

Diverse immune functions of hemocyanins

CJ Coates, J Nairn - Developmental & Comparative Immunology, 2014 - Elsevier
Substantial evidence gathered recently has revealed the multiple functionalities of
hemocyanin. Contrary to previous claims that this ancient protein is involved solely in …

The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins

C Gerdemann, C Eicken, B Krebs - Accounts of chemical research, 2002 - ACS Publications
The crystal structure of catechol oxidase reveals new insight into the functional properties of
the type-3 copper proteins. This class of proteins includes the closely related and better …

[PDF][PDF] Melanin synthesis in microorganisms-biotechnological and medical aspects

P Plonka, M Grabacka - Acta biochimica polonica, 2006 - frontierspartnerships.org
Melanins form a diverse group of pigments synthesized in living organisms in the course of
hydroxylation and polymerization of organic compounds. Melanin production is observed in …

Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism

H Decker, F Tuczek - Trends in biochemical sciences, 2000 - cell.com
The enzymes tyrosinase, catecholoxidase and hemocyanin all share similar active sites,
although their physiological functions differ. Hemocyanins serve as oxygen carrier proteins …

Hemocyanins and invertebrate evolution

KE van Holde, KI Miller, H Decker - Journal of Biological Chemistry, 2001 - ASBMB
The circulatory transport of oxygen is essential for efficient aerobic metabolism in most
animals. A variety of proteins has evolved to facilitate this process. Most familiar are the …