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1

Camba, Acosta Raul O. "Reaction mechanisms of iron-sulfur proteins studied by protein-film voltammetry." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365860.

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2

Fawcett, Sarah E. J. "Reactions of iron-sulfur clusters in proteins." Thesis, University of Oxford, 1998. https://ora.ox.ac.uk/objects/uuid:87b10a8e-67a8-476b-ae20-49e6892051f5.

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This thesis describes the investigation of reactions of iron-sulfur clusters in proteins using direct electrochemistry. The influence of potential on metal uptake to generate the [M3Fe-4S] cluster from the [3Fe-4S] cluster of Desulfovibrio africanus Fd III is studied. The influence of potential was complex: rapid and reversible interconversions (M = Fe and Zn) occurred only between the states [M3Fe-4S]<sup>2+</sup> and [3Fe-4S]<sup>0</sup>, with [3Fe-4S]<sup>1+</sup> having little affinity for M. The [M3Fe-4S]<sup>1+</sup> cubanes and the hyper-reduced [3Fe-4S]<sup>2-</sup> were relatively unr
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3

Morris, Patricia Ann. "EXAFS of non-heme iron containing proteins." Diss., Georgia Institute of Technology, 1986. http://hdl.handle.net/1853/27402.

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4

St, Pierre T. G. "Moessbauer spectroscopic studies of iron-storage proteins." Thesis, University of Liverpool, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.380097.

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5

Valer, Luca. "Histidine ligated Iron-Sulfur Proteins and Peptides." Doctoral thesis, Università degli studi di Trento, 2022. https://hdl.handle.net/11572/355641.

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Iron-sulfur clusters play a fundamental role in biology and are believed to be ancient cofactors that could have played a role in early protometabolic systems. Thus far, redox active, prebiotically plausible iron-sulfur clusters have always been obtained through cysteine coordination to the iron ions. However, extant iron-sulfur proteins can be found to exploit other modes of binding, including ligation by histidine residues, as seen with [2Fe-2S] Rieske and MitoNEET proteins. In this thesis, we investigated the ability of cysteine- and histidine-containing proteins and peptides to coordinate
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6

Maddocks, Sarah Elizabeth. "Iron metabolism in bacteria : examination of the Feo system (Ferrous iron transporter) and Dps-iron storage proteins." Thesis, University of Reading, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.434313.

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7

Le, Brun Nicolas Edward. "Studies of iron centres in bacterioferritin." Thesis, University of East Anglia, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.482780.

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8

Yoon, Taejin. "Functional and structural studies of human frataxin an iron chaperone protein for mitochondrial iron-sulfur cluster and heme biosyntheses /." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1124287807.

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9

Dzikaitė, Vijolė. "Studies of proteins in heme and iron metabolism /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-762-2/.

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10

Tilley, Gareth John. "Electrochemical investigations into iron-sulfur cluster containing proteins." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365300.

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11

George, S. J. "Magnetic circular dichroism studies of iron-sulphur proteins." Thesis, University of East Anglia, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.376059.

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12

Folgosa, Filipe dos Santos. "Structural and mechanistic studies of iron containing proteins." Doctoral thesis, FCT - UNL, 2008. http://hdl.handle.net/10362/1774.

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Dissertação apresentada para obtenção do Grau de Doutor em Bioquímica, ramo de Bioquímica-Física, pela Universidade Nova de Lisboa, Faculdade de Ciências e Tecnologia<br>Over the last few decades a large effort has been done in the structural biochemistry field. This effort is based on the study of some proteins, namely metalloproteins, that contain cofactors and/or active sites with metal ions in their constitution. This thesis will focus on different studies performed in metalloproteins that contain non-heme iron centers. An important point is their relation to oxygen and reactive oxygen
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13

Dizin, Eric Michel. "Insights On Iron-Sulfur Cluster Assembly Donor Proteins." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1208532379.

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14

Ding, Shu. "Thermodynamic studies on iron-sulfur cluster assembly proteins." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1316472363.

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15

Wang, Jian 1966. "Molecular control of iron metabolism in mammalian cells : new insights into iron regulatory proteins." Thesis, McGill University, 2005. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=86063.

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Iron is an essential but potentially harmful metal element. Iron regulatory protein 1 and IRP2 posttranscriptionally control cellular iron homeostasis by binding to iron-responsive elements (IREs). Binding of IRPs to single IRE within 5'-untranslated region (5'-UTR) of ferritin mRNA attenuates biosynthesis of the iron-storage protein by translational repression, while their binding to multiple IREs within 3'-UTR of transferrin receptor 1 (TfR1) mRNA stimulates that of the iron-acquisition protein through mRNA stabilization. IRP1 and IRP2 share extensive homology, but respond to levels o
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16

Stys, Agnieska. "Role of iron regulatory proteins in the regulation of iron metabolism by nitric oxide." Thesis, Paris 11, 2011. http://www.theses.fr/2011PA11T056.

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Les Iron Regulatory Proteins 1 (IRP1/2) sont des protéines cytosoliques qui contrôlent l’homéostasie du fer chez les mammifères. Elles régulent la concentration de fer intracellulaire au niveau post-transcriptionnel, en interagissant spécifiquement avec des motifs appelés iron responsive élément (IREs). Ces motifs sont localisés dans les régions non traduites des ARNm codant notamment pour la ferritine (Ft), la ferroportine (Fpn) et le récepteur de la transferrine (TfR1). L’IRP1 est une protéine bifonctionnelle, majoritairement exprimée sous une forme contenant un centre [4Fe-4S] qui présente
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17

Dunford, Adrian J. "Kinetic studies on synthetic and biological iron-sulfur based clusters." Thesis, University of Newcastle Upon Tyne, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270825.

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18

Adedeji, Dolapo A. Duin Evert C. "Isoprenoid synthesis new roles for iron sulfur clusters /." Auburn, Ala., 2007. http://repo.lib.auburn.edu/Send%2002-04-08/ADEDEJI_DOLAPO_4.pdf.

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19

Wilks, Paula Elizabeth. "Iron-sulphur proteins from bovine heart NADH-ubiquinone oxidoreductase." Thesis, University of Cambridge, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.339592.

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20

Baptista, Joana Morais. "The role of Di-iron proteins in pathogen resistance." Doctoral thesis, Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica, 2012. http://hdl.handle.net/10362/8583.

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Dissertation presented to obtain the Ph.D. degree in Biochemistry<br>Reactive oxygen and nitrogen species (ROS and RNS) are produced by phagocytic cells of the human immune system to attack invading pathogens due to their ability to damage DNA and the metal centres of proteins. In order to survive inside the host, bacteria activate genes that encode detoxifier enzymes, like the Escherichia coli nitric oxide-reductase flavodiiron protein, also known as flavorubredoxin (FlRd), and repairing proteins, such as the E. coli YtfE di-iron protein involved in the recovery of damaged Fe-S centres
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21

Dill, Brian D. "Identification of Chlamydial Iron-Responsive Proteins during Intracellular Growth." Digital Commons @ East Tennessee State University, 2008. https://dc.etsu.edu/etd/1955.

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Chlamydia trachomatis is an obligate intracellular bacterium and the most prevalent cause of bacterial sexually transmitted disease. Genital chlamydial infections, marked by chronic, intense inflammation, can lead to genital tissue scarring and infertility and is a contributing factor to development of pelvic inflammatory disease and ectopic pregnancy. Iron is required as a cofactor for numerous highly conserved pathways, and nearly all studied organisms rely on iron for growth. In response to iron restriction, the chlamydial developmental cycle arrests at the intracellular reticulate body sta
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22

Wu, Shu-Pao. "Iron-sulfur cluster biosynthesis. Iron-sulfur cluster transfer from holo ISU and ISA to apo ferredoxin." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1078866123.

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Thesis (Ph. D.)--Ohio State University, 2004.<br>Title from first page of PDF file. Document formatted into pages; contains xx, 161 p.; also includes graphics Includes bibliographical references (p. 153-161). Available online via OhioLINK's ETD Center
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23

Mansy, Sheref S. "Structure and function of iron-sulfur cluster biosynthesis proteins and the influence of oxygen ligation." Connect to this title online, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1059664189.

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Thesis (Ph. D.)--Ohio State University, 2003.<br>Title from first page of PDF file. Document formatted into pages; contains xxi, 250 p.; also includes graphics (some col.) Includes bibliographical references (p. 226-250). Available online via OhioLINK's ETD Center
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24

Houldershaw, David. "The electrostatics of iron binding to transferrin." Thesis, Birkbeck (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244463.

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25

Bond, Jennifer M. "Investigations on antioxidant defence proteins and peptides." Thesis, Cranfield University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.278723.

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26

Ravindranath, Velaga M. "Elucidating the role of mitoferrin (Mfrn), iron regulatory proteins (IRP1 and IRP2) and hephaestin (Heph) in iron metabolism by tagSNP and protein-protein interaction (PPI) analysis." Thesis, London Metropolitan University, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.639414.

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Precisely how Hephaestin (Heph) facilitate iron release from cells is poorly understood. The work in this thesis tried to establish the role of different iron metabolic proteins, Mitoferrin (Mfrn), IRPs and Heph in iron homeostasis. Analysis of 18 tagSNPs in the Mfrn gene was carried out in an AsianCaucasian population to establish any correlation between the Mfrn tagSNPs, haemoglobin levels and birth weight in the presence of covariates such as sex of the fetus, gestational age and mother's booking weight. Two-way ANCOVA analysis was carried out to check if the covariates have any influence o
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27

Ricard, Michelle. "Iron acquisition from porcine proteins by Actinobacillus pleuropneumoniae biotype 1." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0034/MQ64438.pdf.

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28

Chen, Guohua 1966. "A potential role of iron-regulatory proteins in tumor growth /." Thesis, McGill University, 2005. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=97925.

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Iron is indispensable for cell proliferation and growth, but it is potentially toxic when present in excess. Two homologous iron regulatory proteins (IRP1 and IRP2) control cellular iron homeostasis by binding to iron-responsive elements (IREs) and post-transcriptionally coordinating the expression of transferrin receptor 1 (TfR1) and ferritin. We have previously reported that overexpression of IRP1C437S, a constitutive IRP1 mutant, inhibits H1299 human lung cancer cell growth in vitro. In current study, we investigated the potential role of IRPs in tumor growth in vivo by the injection of H12
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29

Dycke, Camille. "Modulation de l'activité des Iron regulatory proteins par divers mécanismes." Université Joseph Fourier (Grenoble), 2006. http://www.theses.fr/2006GRE10145.

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L'homéostasie du fer est assurée chez les métazoaires au niveau post-transcriptionnel par le système IRE (Iron Responsive Elemenf)/IRP (Iron Responsive Proteins). Les IRP sont des protéines cytosoliques interagissant avec des motifs IRE de l'ARN messager de certaines protéines. En présence de fer, IRP1 intègre un centre [4Fe-4S] et acquiert une activité aconitase, alors qu'IRP2 est rapidement dégradée par le protéasome. IRP1 humaine produite dans la levure Saccharomyces cerevisiae interagit avec les thiorédoxines, suggérant un nouveau mécanisme de régulation de son activité. Un peptide de 73 a
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30

Zhang, Dianzheng. "Cloning, overexpression and characterization of iron regulatory proteins from insects." Diss., The University of Arizona, 2001. http://hdl.handle.net/10150/279922.

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Iron is essential for life and iron homeostasis is important for all species. Compared to the understanding of iron metabolisms in vertebrates, we know much less about insect intracellular iron homeostasis. The iron regulatory proteins (IRPs) play central roles in this process by interaction with iron responsive elements (IREs). Here, I report the cloning, sequencing, overexpression, purification and characterization of IRP1s from two insect species, Manduca sexta and Aedes aegypti. Electrophoretic mobility shift assays demonstrated that both IRP1s specifically bind IREs s not only from the s
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31

Torres, Alfredo Gabriel. "Characterization of the heme transport system in Escherichia coli O157:H7, and importance of iron uptake systems in virulence /." Digital version accessible at:, 1999. http://wwwlib.umi.com/cr/utexas/main.

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32

Im, Sang-Choul. "Redox studies on rubredoxin and [2Fe-2S] proteins." Thesis, University of Newcastle Upon Tyne, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295479.

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33

Thomas, Carla. "The validation and use of the rat intestinal epithelial cell line 6 (IEC-6) to study the role of ferroportin1 and divalent metal transporter 1 in the uptake of iron from Fe(II) and Fe(III)." University of Western Australia. Physiology Discipline Group, 2003. http://theses.library.uwa.edu.au/adt-WU2004.0019.

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[Formulae and special characters can only be approximated here. Please see the pdf version of the abstract for an accurate reproduction.] Iron is vital for almost all living organisms by participating in a wide variety of metabolic processes, including oxygen transport, DNA synthesis, and electron transport. However, iron concentrations in body tissues must be tightly regulated because excessive iron leads to tissue damage, as a result of formation of free radicals. In mammals since no controlled means of eliminating unwanted iron has evolved, body iron balance is maintained by alterations i
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34

Zuccola, Harmon Jay. "The crystal structure of monoferric human serum transferrin." Diss., Georgia Institute of Technology, 1992. http://hdl.handle.net/1853/26304.

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35

Kwan, Miu-fan, and 關妙芬. "Characterization of TM4 of NRAMP1: implication for FEII transport." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2003. http://hub.hku.hk/bib/B29275143.

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36

Al-Massad, Fareeda Khalid Nasser. "Comparative physicochemical & biochemical studies of ferritin & bacterioferritin." Thesis, University of East Anglia, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358458.

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37

Busch, J. L. H. C. "Structural and spectroscopic studies of Desulfovibrio africanus ferrodoxin III." Thesis, University of East Anglia, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267262.

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38

Hunt, Colette. "Magnetic studies of fine particle biological systems." Thesis, University of Liverpool, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359198.

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39

Wisedchaisri, Goragot. "Structural basis for transcription regulations in Mycobacterium tuberculosis by iron-dependent regulator and dormancy survival regulator /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/9269.

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40

He, Didi. "Structural basis for iron (II) metabolism in encapsulated ferritin-like proteins." Thesis, University of Edinburgh, 2017. http://hdl.handle.net/1842/23466.

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Ferritins are ubiquitous proteins that serve the dual-function of iron reservoir and sequestering the Fe(II) toxicity. The function of ferritins totally depends on the characteristic spherical structure with a di-iron centre performing the iron oxidation and a hallow cavity enclosing the iron minerals in a bioavailable form. I have characterised the structure, assembly and function of a new member of ferritin superfamily that is natively enclosed within an encapsulin shell. Encapsulin proteins are structurally-related to a virus capsid and form 60-meric or 180-meric icosahedrons. I show that t
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41

Wardrop, Stacey Leanne. "Regulation of molecules involved in cellular iron homeostasis and transport /." [St. Lucia, Qld.], 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16265.pdf.

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42

Ebert, C. Edward. "Effects of mutations of the iron-sulfur protein on the function and structure of the cytochrome bc₁ complex of yeast mitochondria." Morgantown, W. Va. : [West Virginia University Libraries], 2003. https://etd.wvu.edu/etd/controller.jsp?moduleName=documentdata&jsp%5FetdId=3.

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Thesis (Ph. D.)--West Virginia University, 2003.<br>Title from document title page. Document formatted into pages; contains viii, 144 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 129-144).
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43

Gelling, Cristy Lee Biotechnology &amp Biomolecular Sciences Faculty of Science UNSW. "Tetrahydrofolate and iron-sulfur metabolism in Saccharomyces cerevisiae." Publisher:University of New South Wales. Biotechnology & Biomolecular Sciences, 2008. http://handle.unsw.edu.au/1959.4/43270.

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Tetrahydrofolate-mediated one-carbon metabolism is required for the biosynthesis of many central metabolites, including some amino acids, nucleobases, and nucleotides, and hence dysfunction of one-carbon metabolism is associated with many human diseases and disorders. The mitochondrial glycine decarboxylase complex (GDC) is an important component of one-carbon metabolism, generating 5,10-methylene-tetrahydrofolate (5,10-CH2-H??4folate) from glycine. Previous work has shown that the genes encoding the unique sub-units of the Saccharomyces cerevisiae GDC (GCV1, GCV2 and GCV3) are regulated in
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44

Faraldo-Gómez, José D. "Computational studies of bacterial iron transport proteins : methodological aspects and application." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249243.

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45

Foster, Matthew W. "Biosynthetic assembly and nitric oxide mediated degradation of iron-sulfur proteins /." The Ohio State University, 2000. http://rave.ohiolink.edu/etdc/view?acc_num=osu1488199501404912.

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46

Xu, Xiangcong. "THE MOLECULAR MECHANISMS OF IRON AND FERRITIN METABOLISM IN." University of Sydney, 2008. http://hdl.handle.net/2123/3535.

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Doctor of Philosophy(PhD)<br>Iron (Fe) is essential for cell growth and replication as many Fe-containing proteins catalyse key reactions involved in energy metabolism (cytochromes, mitochondrial aconitase and Fe-S proteins of the electron transport chain), respiration (hemoglobin and myoglobin) and DNA synthesis (ribonucleotide reductase). If not appropriately shielded, Fe could participate in one-electron transfer reactions that lead to the production of extremely toxic free radicals. The Fe storage protein, ferritin, is essential to protect cells against Fe-mediated oxidative stress by acco
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47

Bae, Dong-Hun. "The Effects of Iron Levels on the Interaction between Polyamine Metabolism and Iron Metabolism in Neoplastic Cells." Thesis, The University of Sydney, 2018. http://hdl.handle.net/2123/18081.

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Iron is a crucial element that is associated with many metabolic pathways important for life sustaining processes. Polyamines are small positively charged polycations involved in various physiological functions. Both iron and polyamines levels are known to be high in cancer cells which suggests a possible unexplored link between the two metabolic pathways. For the first time, we demonstrate that iron-depletion robustly regulates the expression of 13 polyamine pathway proteins. Iron-depletion also decreased polyamine and S-adenosylmethionine levels (required for spermidine/spermine biosynthesi
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48

Lugo-Mas, Priscilla. "Synthetic analogues of cysteinate-ligated non-heme iron enzymes : understanding the structure-function relationship of nitrile hydratase (NHase) and superoxide reductase (SOR) /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/8635.

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49

Beard, Collen Alana. "Rubredoxin cobalt substitution and crystallization attempts." Thesis, Georgia Institute of Technology, 1989. http://hdl.handle.net/1853/29863.

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50

Lee, David Andrew. "Computer simulation of a conformational change in lactoferrin." Thesis, Birkbeck (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.368084.

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