Academic literature on the topic 'Cluster [Fe-S]'

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Dissertations / Theses on the topic "Cluster [Fe-S]"

1

Bian, Shumin. "Fe-S proteins : cluster assembly and degradation /." The Ohio State University, 1998. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487952208109007.

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2

Islam, Shams Tania Afroza. "The catalytic properties of Fe-S cluster containing enzymes." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:eba9a2de-52fb-4da8-88e2-1fb0c2f69998.

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Many enzymes contain iron- sulfur (Fe-S) clusters which have a huge impact on their catalytic properties. These clusters may form part of the active site or form an electron relay system from the surface of the protein to the active site. Protein film electrochemistry (PFE) was utilized to elucidate the properties of some Fe-S cluster enzymes, namely, Hyd-1(a hydrogenase with an Fe-S electron relay), PceA (a reductive dehalogenase containing Fe-S clusters to facilitate electron transfer with redox partner) and CODH I<sub>Ch</sub> and CODH II<sub>Ch</sub> (carbon monoxide dehydrogenases with Fe
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3

Luo, Wen-I. "The Role of Chaperones in Iron-Sulfur Cluster Biogenesis." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1325168796.

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4

Puglisi, Rita. "Structural and functional characterization of chaperones in Fe-S cluster biogenesis and regulation." Thesis, King's College London (University of London), 2017. https://kclpure.kcl.ac.uk/portal/en/theses/structural-and-functional-characterization-of-chaperones-in-fes-cluster-biogenesis-and-regulation(b2e55aa5-c7b3-4113-8222-7e856a26a36b).html.

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Dysfunctions in Fe-S protein biogenesis and mitochondrial iron accumulation in heart and neurones are part of the phenotype of a genetic neurodegenerative disease called Friedreich's ataxia. This pathology is caused by the deficiency of a mitochondrial protein, frataxin, highly conserved throughout species and currently thought to be a regulator of Fe-S cluster biosynthesis. The study of the mechanism of Fe-S cluster assembly in mitochondria is important to provide insights and valuable information potentially relevant for the study of iron-storage diseases. The biogenesis of iron sulfur clust
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5

Ramirez, Melissa V. "Probing Plant Metabolism: The Machineries of [Fe-S] Cluster Assembly and Flavonoid Biosynthesis." Diss., Virginia Tech, 2008. http://hdl.handle.net/10919/77167.

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The organization of metabolism is an essential feature of cellular biochemistry. Metabolism does not occur as a linear assembly of freely diffusing enzymes, but as a complex web in which multiple interactions are possible. Because of the crowded environment of the cell, there must be structured and ordered mechanisms that control metabolic pathways. The following work will examine two metabolic pathways, one that is ubiquitous among living organisms and another that is entirely unique to plants, and examine the organization of each in an attempt to further define mechanisms that are fundamenta
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6

Nuth, Manunya. "Mechanism of Fe-S cluster biosynthesis the [2Fe-2S] IscU as a model scaffold /." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1092856116.

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Thesis (Ph. D.)--Ohio State University, 2004.<br>Document formatted into pages. Includes bibliographical references. Abstract available online via OhioLINK's ETD Center; full text release delayed at author's request until 2005 Aug. 18.
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7

Johnson, Deborah Cumaraswamy. "Controlled Expression and Functional Analysis of the Iron-Sulfur Cluster Biosynthetic Machinery in Azotobacter vinelandii." Diss., Virginia Tech, 2006. http://hdl.handle.net/10919/27755.

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A system was developed for the controlled expression of genes in Azotobacter vinelandii by using genomic fusions to the sucrose catabolic regulon. This system was used for the functional analysis of the A. vinelandii isc genes, whose products are involved in the maturation of [Fe-S] proteins. For this analysis the scrX gene, contained within the sucrose catabolic regulon, was replaced by the A. vinelandii iscS, iscU, iscA, hscB, hscA, fdx, iscX gene cluster, resulting in duplicate genomic copies of these genes, one whose expression is directed by the normal isc regulatory elements (Pisc) and
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8

Beilschmidt, Lena Kristina. "Evidences for the non-redundant function of A-type proteins ISCA1 and ISCA2 in iron-sulfur cluster biogenesis." Thesis, Strasbourg, 2014. http://www.theses.fr/2014STRAJ031/document.

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Les centres fer-soufre (Fe-S) sont des cofacteurs protéiques essentiels qui participent à un nombre important de fonctions cellulaires allant du métabolisme de l’ADN à la respiration mitochondriale. L’assemblage des centres Fe-S et leur insertion dans des protéines acceptrices requièrent l’activité d’une machinerie protéique dédiée. Bien que les protéines de la biogenèse des centres Fe-S soient conservées, plusieurs aspects fonctionnels et mécanistiques restent inconnus. Notre travail de thèse a consisté à caractériser les protéines mammifères de type A, ISCA1 et ISCA2, qui sont impliquées dan
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9

Jayawardhana, W. Geethamala Dhananjalee. "Investigation of the Influence of Transition Metal Ions on the Fe-S Cluster Biosynthesis Protein SufU." Bowling Green State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1448034834.

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10

Selvaraj, Brinda. "Biochemical and structural studies of 4-hydroxyphenylacetate decarboxylase and its activating enzyme." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://dx.doi.org/10.18452/17052.

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Strikt anaerobe Bakterien wie Clostridium difficile und C. scatologenes verwenden GRE, um die chemisch ungünstige Decarboxylierung von 4-Hydroxyphenylacetat zu p-Cresol zu katalysieren. Das Enzymsystem besteht aus einer Decarboxylase und dem zugehörigen Aktivierungsenzym. Die 4-Hydroxyphenylacetat-Decarboxylase (4Hpad) besitzt zusätzlich zum Protein-basierten Glycinradikal eine weitere Untereinheit mit bis zu zwei [4Fe-4S] Clustern und repräsentiert hierdurch eine neue Klasse von Fe/S-Cluster-haltigen GREs, die aromatische Verbindungen umsetzen. Das Aktivierungsenzym (4Hpad-AE) weicht vom St
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