Download or read book Electrochemical Investigations Into Iron sulfur Cluster Containing Proteins written by Gareth John Tilley and published by . This book was released on 2001 with total page 568 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Electrochemical Studies of Metal sulfur Clusters in Proteins written by Julea Nicole Butt and published by . This book was released on 1993 with total page 744 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Iron Sulfur Clusters in Chemistry and Biology written by Tracey Rouault and published by Walter de Gruyter GmbH & Co KG. This book was released on 2014-08-20 with total page 672 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume on iron-sulfur proteins includes chapters that describe the initial discovery of iron-sulfur proteins in the 1960s to elucidation of the roles of iron sulfur clusters as prosthetic groups of enzymes, such as the citric acid cycle enzyme, aconitase, and numerous other proteins, ranging from nitrogenase to DNA repair proteins. The capacity of iron sulfur clusters to accept and delocalize single electrons is explained by basic chemical principles, which illustrate why iron sulfur proteins are uniquely suitable for electron transport and other activities. Techniques used for detection and stabilization of iron-sulfur clusters, including EPR and Mossbauer spectroscopies, are discussed because they are important for characterizing unrecognized and elusive iron sulfur proteins. Recent insights into how nitrogenase works have arisen from multiple advances, described here, including studies of high-resolution crystal structures. Numerous chapters discuss how microbes, plants, and animals synthesize these complex prosthetic groups, and why it is important to understand the chemistry and biogenesis of iron sulfur proteins. In addition to their vital importance in mitochondrial respiration, numerous iron sulfur proteins are important in maintenance of DNA integrity. Multiple rare human diseases with different clinical presentations are caused by mutations of genes in the iron sulfur cluster biogenesis pathway. Understanding iron sulfur proteins is important for understanding a rapidly expanding group of metabolic pathways important in all kingdoms of life, and for understanding processes ranging from nitrogen fixation to human disease.
Download or read book Chemical and Physical Studies of Iron sulfur Proteins written by Judith R. Bale and published by . This book was released on 1974 with total page 478 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Iron sulfur Clusters in Chemistry and Biology written by Tracey A. Rouault and published by . This book was released on 2017 with total page 447 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Iron Sulfur Proteins Advances in Research and Application 2011 Edition written by and published by ScholarlyEditions. This book was released on 2012-01-09 with total page 60 pages. Available in PDF, EPUB and Kindle. Book excerpt: Iron-Sulfur Proteins: Advances in Research and Application: 2011 Edition is a ScholarlyBrief™ that delivers timely, authoritative, comprehensive, and specialized information about Iron-Sulfur Proteins in a concise format. The editors have built Iron-Sulfur Proteins: Advances in Research and Application: 2011 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Iron-Sulfur Proteins in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Iron-Sulfur Proteins: Advances in Research and Application: 2011 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Download or read book Iron Sulfur Proteins written by and published by Academic Press. This book was released on 1999-06-07 with total page 525 pages. Available in PDF, EPUB and Kindle. Book excerpt: Advances in Inorganic Chemistry presents timely and informative summaries of the current progress in a variety of subject areas within inorganic chemistry, ranging from bioinorganic to solid state. This acclaimed serial features reviews written by experts in the area and is an indispensable reference to advanced researchers. Each volume of Advances in Inorganic Chemistry contains an index, and each chapter is fully referenced.
Download or read book Handbook on Metalloproteins written by Ivano Bertini and published by CRC Press. This book was released on 2001-06-29 with total page 1382 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Novel Iron sulphur Clusters Chemistry written by Jacques Louis Jean Breton and published by . This book was released on 1993 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands written by Marie Bergner and published by Cuvillier Verlag. This book was released on 2017-12-07 with total page 198 pages. Available in PDF, EPUB and Kindle. Book excerpt: Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in recent years. This work uses synthetic [2Fe-2S] analogues to explore the role alternative ligands play in determining the reactivity of iron sulfur clusters. Isomerization in a homoleptically coordinated cluster utilizing a mixed nitrogen- and sulfur-donating ligand is investigated as a model for ligand rearrangement processes during iron sulfur cluster biogenesis. Furthermore, a high fidelity model system for the asymmetrically ligated [2Fe-2S] cluster of mitoNEET proteins is developed and characterized in detail. This cluster and its homoleptic analogue are studied as reagents in proton coupled electron transfer processes, highlighting the role asymmetry and reorganization energy play in tuning this reactivity. The effects of the ligation pattern on entropic contributions during reduction are probed by temperature dependent electrochemical measurements. Finally, synthetic [2Fe-2S] clusters are investigated with respect to their reactivity with organic radicals, mimicking the unique reactivity of biotin synthase.
Download or read book Elucidating Molecular Mechanisms of Iron Sulfur Protein Maturation Mediated by the Cytosolic Iron Sulfur Cluster Assembly Pathway written by Xiaorui Fan and published by . This book was released on 2022 with total page 96 pages. Available in PDF, EPUB and Kindle. Book excerpt: Iron-sulfur (Fe-S) proteins are proteins containing the omnipresent Fe-S clusters as cofactors. Studies have accumulated demonstrating that Fe-S proteins are involved in a plethora of essential cellular functions. In eukaryotes, the cytosolic iron-sulfur cluster assembly (CIA) pathway, which depends on the mitochondrial iron-sulfur cluster assembly (ISC) pathway, facilitates Fe-S cluster incorporation into extramitochondrial Fe-S proteins. These include nuclear proteins required for DNA replication and DNA damage repair, as well as cytosolic proteins required for maintaining cellular iron homeostasis and ribosomal functions. In the CIA pathway, [4Fe-4S] cluster are assembled on the CIA scaffold complex, transferred to CIAO3, and incorporated into CIA substrates via the CIA targeting complex. The maturation of CIA substrates is controlled by cellular iron and oxygen. We demonstrate in this study that the incorporation of CIAO3 into CIA machineries is iron regulated, which may account for this precise control of substrate maturation. We developed a targeted proteomics assay to monitor the presence and abundance of known CIA components and prototypical substrates. Using this assay, we were able to detect that the CIA targeting complex and CIA substrates associated with NUBP2, a component of the CIA scaffold complex. This suggests the possible formation of higher order meta complexes composed of the CIA scaffold complex, CIAO3, the CIA targeting complex and CIA substrates. We show that the interaction between CIAO3 and the CIA scaffold complex is affected by cellular iron availability, and this interaction is additionally strengthened under hypoxic environments and weakened by reactive oxygen species. Furthermore, we found that CIAO3 integration into CIA machineries demands a functional ISC pathway. Moreover, we generated CIAO3 mutants defective in Fe-S cluster binding and observed reduced interactions with both the CIA scaffold complex and the CIA targeting complex. However, stronger interactions with substrates were observed in these mutants, suggesting that CIAO3 and CIA substrates may be present in complexes in the absence of the CIA targeting complex. Lastly, we revealed that the CIAO3 mutant that associates with pulmonary arteriovenous malformations is incapable of integrating into the CIA machineries, which may partially explain the pathological outcome of this mutation. Together, these findings demonstrate the reorganization of the CIA machinery in different cellular environments. Alongside this, we investigated the architecture of the CIA targeting complex with crosslinking mass spectrometry and found that CIAO2B is in contact with the C-terminus of MMS19. A CIA substrate, CDKAL1, is also in close proximity to the C-terminus of MMS19.
Download or read book Iron Sulfur Protein Research written by Hiroshi Matsubara and published by . This book was released on 1987 with total page 350 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Journal of Research of the National Institute of Standards and Technology written by and published by . This book was released on 1991-10 with total page 690 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Spectroscopic and Electrochemical Analysis of the Rieske Iron Sulfur Protein of the Rhodobacter Sphaeroides Bc1 Complex written by and published by . This book was released on 2005 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Comprehensive Treatise of Electrochemistry written by Peter Horsman and published by Springer Science & Business Media. This book was released on 2013-11-11 with total page 552 pages. Available in PDF, EPUB and Kindle. Book excerpt: 1.1. Definition of Terms-Thrombosis, Thromboembolic Disease, Atherosclerosis, and Blood Clotting The terms heart attack or myocardial infarction are more commonly used than thrombosis. The infarct-muscle destruction is simply the end result and thrombosis is the real cause of the heart attack. Thrombosis may be defined as the process of formation of a coalescent or agglutinated solid mass of blood components in the blood stream. Thrombi formed in either arteries or veins often cause occlusion in the vascular system and prevent blood flow. Obstruc to the blood vessel usually occurs at the site where the thrombi deposit. tion Furthermore, thrombi may break loose, travel through the circulating blood stream, and cause obstruction at some distal point of narrowing elsewhere. The mass or thrombus that moves is referred to as an "embolus." The two phenomena are lumped together under the term thromboembolic disease. Thrombosis that reduces blood supply to the heart is the primary factor in heart attacks.
Download or read book Theoretical Investigations of Iron sulfur Proteins written by Brian Wayne Beck and published by . This book was released on 1997 with total page 578 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Insights on Iron sulfur Cluster Assembly Donor Proteins written by Eric Michel Dizin and published by . This book was released on 2008 with total page 113 pages. Available in PDF, EPUB and Kindle. Book excerpt: Abstract: Iron-sulfur clusters are an important class of prosthetic group involved in electron transfer, enzyme catalysis, and regulation of gene expression. Their biosynthesis requires a complex machinery located within the mitochondrion since free iron and sulfide are extremely toxic to the cell. This research has focused on the three central proteins dedicated to the assembly: a cysteine desulfurase, Nfs1, an iron donor protein, frataxin, and an iron-sulfur cluster scaffold protein, Isu1. Human Nfs1, a PLP dependent enzyme, catalyzes the decomposition of cysteine to alanine and forms a persulfide bond with a conserved cysteine residue. To date, Nfs1 has only been partially characterized. Furthermore, its hyperproduction relies on yeast organism, Pichia pastoris, which is cumbersome and leads to quite low yields. Therefore, we undertook to design a bacterial expression system by cloning and overexpressing the gene in different E. coli strain. This enabled only a partial characterization of the cysteine desulfurase. Besides being an iron donor for iron-sulfur cluster assembly, frataxin has also been implicated in heme biosynthesis, and in iron storage in the mitochondrion with reported ferroxidase activity. We decided to further investigate its ability to bind to other metals, such as magnesium, calcium, and zinc, and also studied its ferroxidase activity as a mature and as a truncated protein. We concluded that frataxin has negligible ferroxidase activity, comparable to iron, and quite distinct from ferritin. Moreover frataxin binds zinc besides iron, but with a different stoichiometry.
