Multi-copper Oxidases
Multi-copper Oxidases

Author: Albrecht Messerschmidt

Publisher: World Scientific

Published: 1997-06-12

Total Pages: 477

ISBN-13: 9814498807

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The biological activation of dioxygen is a key reaction in biological systems. Enzymes involved in direct oxygen activation are oxidases and oxygenases. Multi-copper oxidases are an important class of oxidases reducing dioxygen in a four-electron reduction to water with concomitant one-electron oxidation of the reducing substrate. The progress in the characterization and understanding of the structure and function of these enzymes has advanced so tremendously over the last ten years that the publication of a book documenting these achievements has been overdue.Especially the recent discovery of a key role of the FET3 protein of Saccharomyces cerevisae, a multi-copper oxidase, in iron metabolism of this eukaryote has underpinned the function of the plasma multi-copper oxidase ceruloplasmin in vetebrate iron transport. The lately determined x-ray structure of human ceruloplasmin confirms its close structural relatedness to the plant multi-copper oxidases ascorbate oxidase and laccase and due to strong amino-acid sequence similarities has allowed to construct a useful model of the more distantly related blood-clotting factor VIII.This book contains review articles from experts in the field, dealing with modern spectroscopy, enzyme kinetics, bioinorganic chemistry, x-ray crystallography, electron transfer reactions, molecular biology, medical aspects and potential industrial applications of the three main members of multi-copper oxidases, i.e., laccase, ascorbate oxidase and ceruloplasmin.

Multi-copper Oxidases
Multi-copper Oxidases

Author: Albrecht Messerschmidt

Publisher: World Scientific

Published: 1997

Total Pages: 477

ISBN-13: 9810227116

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The biological activation of dioxygen is a key reaction in biological systems. Enzymes involved in direct oxygen activation are oxidases and oxygenases. Multi-copper oxidases are an important class of oxidases reducing dioxygen in a four-electron reduction to water with concomitant one-electron oxidation of the reducing substrate. The progress in the characterization and understanding of the structure and function of these enzymes has advanced so tremendously over the last ten years that the publication of a book documenting these achievements has been overdue.Especially the recent discovery of a key role of the FET3 protein of Saccharomyces cerevisae, a multi-copper oxidase, in iron metabolism of this eukaryote has underpinned the function of the plasma multi-copper oxidase ceruloplasmin in vetebrate iron transport. The lately determined x-ray structure of human ceruloplasmin confirms its close structural relatedness to the plant multi-copper oxidases ascorbate oxidase and laccase and due to strong amino-acid sequence similarities has allowed to construct a useful model of the more distantly related blood-clotting factor VIII.This book contains review articles from experts in the field, dealing with modern spectroscopy, enzyme kinetics, bioinorganic chemistry, x-ray crystallography, electron transfer reactions, molecular biology, medical aspects and potential industrial applications of the three main members of multi-copper oxidases, i.e., laccase, ascorbate oxidase and ceruloplasmin.

Copper-Containing Molecules
Copper-Containing Molecules

Author: Joan S. Valentine

Publisher: Academic Press

Published: 2002-11-01

Total Pages: 493

ISBN-13: 0080544061

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A wide range of researchers are currently investigating different properties and applications for copper-containing proteins. Biochemists researching metal metabolism in organisms ranging from bacteria to plants to animals are working in a completely different area of discovery than scientists studying the transportation and regulation of minerals and small molecule nutrients. They are both working with copper-containing proteins, but in very different ways and with differing anticipated outcomes.

Characterization of Multicopper Oxidase-related Protein and Multicopper Oxidase-1 in Insects
Characterization of Multicopper Oxidase-related Protein and Multicopper Oxidase-1 in Insects

Author: Zeyu Peng

Publisher:

Published: 2014

Total Pages:

ISBN-13:

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Typical multicopper oxidases (MCOs) have ten conserved histidines and one conserved cysteine that coordinate four copper atoms, which are required for oxidase activity. During our studies of insect MCOs, we discovered a gene that we named multicopper oxidase-related protein (MCORP). MCORPs share sequence identity with MCOs, but lack many of the copper-coordinating residues. We identified MCORP orthologs in many insect species, but not in other invertebrates or vertebrates. We purified recombinant Tribolium castaneum (red flour beetle) MCORP. As expected, no oxidase activity was detected. We analyzed expression profiles of TcMCORP and Anopheles gambiae (African malaria mosquito) MCORP. They are constitutively expressed at a low level in many tissues, including ovaries. TcMCORP larval RNAi led to 100% mortality before adult stage. These deaths occurred during the larval to pupal and pupal to adult molts. Pharate pupal RNAi resulted in 20% mortality during the pupal to adult molt, and 100% mortality by one month after adult eclosion. In addition, knockdown of TcMCORP in females prevented oocyte maturation, thus greatly decreasing the number of eggs laid. These results indicate that TcMCORP is an essential gene and that its function is required for reproduction. An understanding of the role MCORP plays in insect physiology may help to develop new strategies for controlling insect pests. A multicopper oxidase-1 (MCO1) ortholog has been identified in all insect species examined so far; thus, MCO1 probably has a conserved physiological function in insects. Most of the well-studied MCOs are laccases, ferroxidases, or ascorbate oxidases. Previously we found Drosophila melanogaster MCO1 has ferroxidase activity and we identified three putative iron binding residues in DmMCO1. Our kinetic analysis of recombinant MCO1 from Drosophila melanogaster, Anopheles gambiae, Tribolium castaneum and Manduca sexta showed that MCO1 orthologs are much better at oxidizing ascorbate than laccase substrates or ferrous iron, suggesting that MCO1 orthologs function as ascorbate oxidases. The putative iron binding residues are required for ascorbate oxidase activity but not ferroxidase and laccase activities. Ascorbate oxidases have been identified only in plants. This is the first identification of ascorbate oxidase in insects. Further studies are needed to understand their physiological function in insects.

Copper Amine Oxidases
Copper Amine Oxidases

Author: Giovanni Floris

Publisher: CRC Press

Published: 2009-06-01

Total Pages: 356

ISBN-13: 1420076817

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Although the amount of research on copper amine oxidases has grown rapidly and substantially in the past decade, the field unfortunately suffers from lack of cohesion and significant confusion surrounds aspects as simple as confirmation of enzyme identities. This book describes the structure of the enzymes, the role of copper, and of the unusual co

Copper-Oxygen Chemistry
Copper-Oxygen Chemistry

Author: Kenneth D. Karlin

Publisher: John Wiley & Sons

Published: 2011-08-24

Total Pages: 417

ISBN-13: 1118094352

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Covers the vastly expanding subject of oxidative processes mediated by copper ions within biological systems Copper-mediated biological oxidations offer a broad range of fundamentally important and potentially practical chemical processes that cross many chemical and pharmaceutical disciplines. This newest volume in the Wiley Series on Reactive Intermediates in Chemistry and Biology is divided into three logical areas within the topic of copper/oxygen chemistry— biological systems, theory, and bioinorganic models and applications—to explore the biosphere for its highly evolved and thus efficient oxidative transformations in the discovery of new types of interactions between molecular oxygen and copper ion. Featuring a diverse collection of subject matter unified in one complete and comprehensive resource, Copper-Oxygen Chemistry probes the fundamental aspects of copper coordination chemistry, synthetic organic chemistry, and biological chemistry to reveal both the biological and chemical aspects driving the current exciting research efforts behind copper-oxygen chemistry. In addition, Copper-Oxygen Chemistry: Addresses the significantly increasing literature on oxygen-atom insertion and carbon-carbon bond-forming reactions as well as enantioselective oxidation chemistries Progresses from biological systems to spectroscopy and theory, and onward to bioinorganic models and applications Covers a wide array of reaction types such as insertion and dehydrogenation reactions that utilize the cheap, abundant, and energy-containing O2 molecule With thorough coverage by prominent authors and researchers shaping innovations in this growing field, this valuable reference is essential reading for bioinorganic chemists, as well as organic, synthetic, and pharmaceutical chemists in academia and industry.