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In biochemistry, a metalloprotein is a generic term for a protein that contains a metal cofactor. The metal may be an isolated ion or may be coordinated with a nonprotein organic compound, such as the porphyrin found in hemoproteins. In some cases, the metal is co-coordinated with a side chain of the protein and an inorganic nonmetallic ion. This kind of protein-metal-nonmetal structure is seen in iron-sulfur clusters Metalloproteins deals with all aspects related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The biological roles of metal cations and metal-binding proteins are endless. They are involved in all crucial cellular activities. Many pathological conditions are related to the problematic metal metabolism. Research in metalloprotein-related topics is therefore rapidly growing, and different aspects of metal-binding proteins progressively enter curricula at Universities and even at the High School level on occasion. However, no key resource providing basic, but comprehensible knowledge on this rapidly expanding field exists. The Encyclopedia of Metalloproteins aims to bridge this gap, and will attempt to cover various aspects of metalloprotein/metalloproteomics and will deal with the different issues related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The goal is to cover exhaustively all catalytically and biologically crucial metal ions and to find at least one interacting protein for other metal ions. The Encyclopedia of Metalloproteins will provide a key resource for advanced undergraduate and graduate students, researchers, instructors, and professors interested in protein science, biochemistry, cell biology, and genetics.
This volume provides an up-to-date, in-depth overview of the methods that have been applied to studying the complex metalloproteins at a molecular level. Chapters cover a wide range of approaches focusing on genetic, biochemical, spectroscopic, chemical methods, and theoretical calculations. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Metalloproteins: Methods and Protocols aims to be useful for anyone who is interested in metalloprotein research and wants to address the unanswered mechanistic and biosynthetic questions of these fascinating enzyme systems.
Numerous essential biological functions involve metalloproteins; therefore, understanding metalloproteins and how to manipulate them is significant in the biological and medical fields. An examination of current research, Metalloproteins: Theory, Calculations, and Experiments explores the interplay between theory and experiment, detailing the role
Metalloproteins and Motor Proteins, Volume 141 focuses on recent advances in studying metalloproteins and motor proteins, along with their roles in different pathologies and drug-resistance. Chapters include Transcriptomic Analysis Reveals Zinc-Mediated Virulence and Pathogenicity in Multidrug-Resistant Acinetobacter baumannii, The Mechanistic Insights into Different Aspects of Promiscuity in Metalloenzymes, Role of Metal ion in ion channel Mechanisms, A model of microtubule depolymerization by kinesin-8 motor proteins, Metalloproteins and metalloproteomics in health and disease, Decoding Genetic and Pathophysiological Mechanisms in Amyotrophic Lateral Sclerosis and Primary Lateral Sclerosis: A Comparative Study of Differentially Expressed Genes and Implicated Pathways in Motor Neuron Disorders, and much more.Additional chapters cover Exploring the effect of disease causing mutations in metal binding sites of human ARSA in Metachromatic Leukodystrophy, Role of transmembrane proteins in regulating metalloproteins and motor proteins in human cancer, Role of transmembrane proteins in metalloproteins and motor proteinsin human neurogenesis, Role of transmembrane proteins in metalloproteins and motor proteins in human aging, Vesicle transport of metalloproteinases, Motor proteins and spermatogenesis, and much more. - Integrates experimental and computational methods for studying structure and function of metalloproteins and motor proteins and their implication in drug design - Presents timely chapters written by well-renowned authorities in their field - Contains a high number of high quality illustrations, figures, and tables and targets a very wide audience of specialists, researchers, and students
Summarizes the essential biosynthetic pathways for assembly of metal cofactor sites in functional metalloproteins Metalloprotein Active Site Assembly focuses on the processes that have evolved to orchestrate the assembly of metal cofactor sites in functional metalloproteins. It goes beyond the simple incorporation of single metal ions in a protein framework, and includes metal cluster assembly, metal-cofactor biosynthesis and insertion, and metal-based post-translational modifications of the protein environments that are necessary for function. Several examples of each of these areas have now been identified and studied; the current volume provides the current state-of-the-art understanding of the processes involved. An excellent companion to the earlier book in this series Metals in Cells—which discussed both the positive and negative effects of cellular interactions with metals—this comprehensive book provides a diverse sampling of what is known about metalloprotein active site assembly processes. It covers all major biological transition metal components (Mn, Fe, Co, Ni, Mo), as well as the other inorganic components, metal-binding organic cofactors (e.g., heme, siroheme, cobalamin, molybdopterin), and post-translationally modified metal binding sites that make up the patchwork of evolved biological catalytic sites. The book compares and contrasts the biosynthetic assembly of active sites involving all biological metals. This has never been done before since it is a relatively new, fast-developing area of research. Metalloprotein Active Site Assembly is an ideal text for practitioners of inorganic biochemistry who are studying the biosynthetic pathways and gene clusters involved in active site assembly, and for inorganic chemists who want to apply the concepts learned to potential synthetic pathways to active site mimics.
Numerous essential biological functions involve metalloproteins; therefore, understanding metalloproteins and how to manipulate them is significant in the biological and medical fields. An examination of current research, Metalloproteins: Theory, Calculations, and Experiments explores the interplay between theory and experiment, detailing the role
This Handbook on Metalloproteins focuses on the available structural information of proteins and their metal ion coordination spheres. It centers on the metal ions indispensable for life but also considers metal ions used as substitution probes in studies of metalloproteins. Emphasizing the structure-function relationship, the book covers the common and distinct characterstics of metallo- enzymes, proteins, and amino acids bonded to copper, zinc, iron, and more.
De Novo Enzyme Design, the newest volume in the Methods in Enzymology series, continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume includes the design of metal binding maquettes, insertion of non-natural cofactors, Cu metallopeptides, non-covalent interactions in peptide assemblies, peptide binding and bundling, heteronuclear metalloenzymes, florinated peptides, De Novo imaging agents, and protein-protein interaction. - Continues the legacy of this premier serial with quality chapters on de novo enzyme design - Represents the newest volume in the Methods in Enzymology series, providing premier, quality chapters authored by leaders in the field - Ideal reference for those interested in the study of enzyme design that looks at both structure and mechanism
Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms. This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community with an overview of high-resolution EPR and its application to metals in biology. This volume, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, covers high-resolution EPR methods, iron proteins, nickel and copper enzymes, and metals in medicine. An eloquent synopsis of each chapter is provided by John Pilbrow in the Introduction. A second volume, Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes, will appear later this year covering the complement of other metalloproteins. One of the pioneers in the development of pulsed EPR and its application to metalloproteins was Arthur Schweiger, whose contribution we include in this volume. Unfortunately, he passed away suddenly during the preparation of this volume. The editors and coauthors are extremely honored to dedicate this volume to the memory of Arthur Schweiger in recognition of his technical advances and insights into pulsed EPR and its application to metalloproteins. Arthur was extremely humble and treated everyone with equal respect. He was a gifted educator with an ability to explain complex phenomena in terms of simple intuitive pictures, had a delightful personality, and continues to be sadly missed by the community. It is an honor for the editors to facilitate the dissemination of these excellent contributions to the scientific community. Suggestions for future volumes are always appreciated.