Auswahl der wissenschaftlichen Literatur zum Thema „[4Fe-4S]2+“
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Zeitschriftenartikel zum Thema "[4Fe-4S]2+"
Azam, Tamanna, Jonathan Przybyla-Toscano, Florence Vignols, Jérémy Couturier, Nicolas Rouhier und Michael K. Johnson. „[4Fe-4S] cluster trafficking mediated by Arabidopsis mitochondrial ISCA and NFU proteins“. Journal of Biological Chemistry 295, Nr. 52 (29.10.2020): 18367–78. http://dx.doi.org/10.1074/jbc.ra120.015726.
Der volle Inhalt der QuelleDuan, Xuewu, Juanjuan Yang, Binbin Ren, Guoqiang Tan und Huangen Ding. „Reactivity of nitric oxide with the [4Fe–4S] cluster of dihydroxyacid dehydratase from Escherichia coli“. Biochemical Journal 417, Nr. 3 (16.01.2009): 783–89. http://dx.doi.org/10.1042/bj20081423.
Der volle Inhalt der QuelleSutton, Victoria R., Erin L. Mettert, Helmut Beinert und Patricia J. Kiley. „Kinetic Analysis of the Oxidative Conversion of the [4Fe-4S]2+ Cluster of FNR to a [2Fe-2S]2+ Cluster“. Journal of Bacteriology 186, Nr. 23 (01.12.2004): 8018–25. http://dx.doi.org/10.1128/jb.186.23.8018-8025.2004.
Der volle Inhalt der QuelleGeorge, S. J., F. A. Armstrong, E. C. Hatchikian und A. J. Thomson. „Electrochemical and spectroscopic characterization of the conversion of the 7Fe into the 8Fe form of ferredoxin III from Desulfovibrio africanus. Identification of a [4Fe–4S] cluster with one non-cysteine ligand“. Biochemical Journal 264, Nr. 1 (15.11.1989): 275–84. http://dx.doi.org/10.1042/bj2640275.
Der volle Inhalt der QuelleAzam, Tamanna, Jonathan Przybyla-Toscano, Florence Vignols, Jérémy Couturier, Nicolas Rouhier und Michael K. Johnson. „The Arabidopsis Mitochondrial Glutaredoxin GRXS15 Provides [2Fe-2S] Clusters for ISCA-Mediated [4Fe-4S] Cluster Maturation“. International Journal of Molecular Sciences 21, Nr. 23 (03.12.2020): 9237. http://dx.doi.org/10.3390/ijms21239237.
Der volle Inhalt der QuelleDridge, Elizabeth J., Carys A. Watts, Brian J. N. Jepson, Kirsty Line, Joanne M. Santini, David J. Richardson und Clive S. Butler. „Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy“. Biochemical Journal 408, Nr. 1 (29.10.2007): 19–28. http://dx.doi.org/10.1042/bj20070669.
Der volle Inhalt der QuelleBUSCH, Johanneke L. H., Jacques L. BRETON, Barry M. BARTLETT, Fraser A. ARMSTRONG, Richard JAMES und Andrew J. THOMSON. „[3Fe-4S]↔[4Fe-4S] cluster interconversion in Desulfovibrio africanus ferredoxin III: properties of an Asp14→Cys mutant“. Biochemical Journal 323, Nr. 1 (01.04.1997): 95–102. http://dx.doi.org/10.1042/bj3230095.
Der volle Inhalt der QuelleSmith, Eugene T., Dennis W. Bennett und Benjamin A. Feinberg. „Redox properties of 2[4Fe4S] ferredoxins“. Analytica Chimica Acta 251, Nr. 1-2 (Oktober 1991): 27–33. http://dx.doi.org/10.1016/0003-2670(91)87111-j.
Der volle Inhalt der QuelleRoland, Mélanie, Jonathan Przybyla-Toscano, Florence Vignols, Nathalie Berger, Tamanna Azam, Loick Christ, Véronique Santoni et al. „The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins“. Journal of Biological Chemistry 295, Nr. 6 (06.01.2020): 1727–42. http://dx.doi.org/10.1074/jbc.ra119.011034.
Der volle Inhalt der QuelleStripp, Sven T., Jonathan Oltmanns, Christina S. Müller, David Ehrenberg, Ramona Schlesinger, Joachim Heberle, Lorenz Adrian, Volker Schünemann, Antonio J. Pierik und Basem Soboh. „Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly“. Biochemical Journal 478, Nr. 17 (07.09.2021): 3281–95. http://dx.doi.org/10.1042/bcj20210224.
Der volle Inhalt der QuelleDissertationen zum Thema "[4Fe-4S]2+"
Davasse, Valérie. „Ingénierie de la ferredoxine 2[4Fe-4S] de Clostridium pasteurianum“. Grenoble 1, 1993. http://www.theses.fr/1993GRE10135.
Der volle Inhalt der QuelleLenormand-Foucaut, Alix. „Modélisation chimique de protéines fer-soufre à haut potentiel : synthèses et caractérisations physico-chimiques de nouveaux agrégats à ligands thiolates encombrés dans les états (4Fe-4S)2+ et (4Fe-4S)3+“. Université Joseph Fourier (Grenoble), 1996. http://www.theses.fr/1996GRE10056.
Der volle Inhalt der QuelleMaerker, Claudia. „Die zwei metabolischen Funktionen der Aconitase AcoA aus Aspergillus nidulans Aconitase-Aktivität im (4Fe-4S)2+ und Methylisocitrat-Dehydratase-Aktivität im (3Fe-4S)+-Zustand /“. [S.l.] : [s.n.], 2007. http://deposit.ddb.de/cgi-bin/dokserv?idn=98410786X.
Der volle Inhalt der QuelleChan, Alice. „Structure et Mécanisme de la Quinolinate Synthase : enzyme à centre [4Fe-4S]2+ et cible d'agents antibactériens“. Thesis, Grenoble, 2014. http://www.theses.fr/2014GRENV036.
Der volle Inhalt der QuelleThe Nicotinamide Adenine Dinucleotide (NAD) is a key cofactor essential for cellular metabolism. Synthesized from quinolinic acid (QA) in all living organisms, NAD biosynthesis is different between eucaryotes and procaryotes. Indeed, most of eukaryotes produce QA from L-tryptophan, whereas most of prokaryotes and plants synthesize QA by the concerted action of 2 enzymes: L-aspartate oxydase (NadB), an FAD enzyme, which catalyzes L-Aspartate oxidation to form iminoaspartate (IA) while quinolinate synthetase (NadA) allows condensation between IA and Dihydroxyacetone Phosphate (DHAP) to produce QA. Besides this « de novo » pathway, most eukaryotes and some bacteriae have a salvage pathway which allows NAD synthesis from nutrients and metabolites of NAD degradation in order to maintain a correct pool of NAD in the cell. However, some pathogens like Mycobacterium leprae, Helicobacter pylori do not possess this pathway. As a consequence, NadA represents a very attractive target for designing specific antibacterial agents since it does not exist in Human.NadA is the only metalloenzyme of NAD de novo biosynthesis whose molecular mechanism and tridimensional structure with its [4Fe-4S]2+ cluster are unknown. Using substrate and intermediate analogues, we have been able to understand better NadA mechanism, especially [4Fe-4S]2+ cluster role in catalysis. Moreover, we proposed the first in vitro and in vivo inhibitor of NadA : the 4,5 Dithiohydroxyphtalic Acid (DTHPA) which gave us basis to design powerful and specific NadA inhibitors thanks to a structure-activity relationship study. Besides, we resolved the first X-rays structure of NadA under its holoprotein form. Datas we extracted from it helped us greatly to understand NadA mechanism
Lawson, Daku Latévi Maxime. „Étude de la protéine fer-soufre à haut potentiel de Chromatium vinosum et de composés modèles : structures électroniques dans les états d'oxydation [4Fe-4S]2+ et [4Fe-4S]3+ en relation avec les données d'aimantation et des mesures optiques à température variable“. Grenoble 1, 1999. http://www.theses.fr/1999GRE10072.
Der volle Inhalt der QuelleJobelius, Hannah. „Etude de la métalloenzyme IspH, une cible pour le développement de nouveaux agents antibactériens“. Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAF004.
Der volle Inhalt der QuelleIspH is the last enzyme of the methylerythritol phosphate pathway which produces the two precursors needed for the biosynthesis of all isoprenoids. This metalloenzyme is essential for the survival of many microorganisms, among them pathogenic bacteria and the parasite responsible for malaria. Being absent in humans, IspH is a suitable target for the development of novel antimicrobial agents. Using a multidisciplinary approach combining molecular biology, enzymology, Raman and Mössbauer spectroscopy, and crystallography, the objective of this thesis was to understand the mechanism of IspH and especially the formation of the two products in a defined ratio. Several mutants were produced, studied and characterized, and the results shed light on some amino acids which are important for the enzyme activity and for maintaining the ratio of the two products. During biophysical studies, these mutants revealed differences in their cofactor, a [4Fe4S]2+ cluster, and in their way to bind the substrate as compared to the wild type enzyme. IspH has for the first time been studied using Raman spectroscopy and a detailed analysis was conducted
Hinkley, Glen Thomas. „Ligand effects on the reduction potential of the [4Fe-4S] cluster in Lysine 2, 3-aminomutase“. 2005. http://catalog.hathitrust.org/api/volumes/oclc/64033202.html.
Der volle Inhalt der QuelleLin, Zong-Sian, und 林宗憲. „Transformation of Dinitrosyl Iron Complexes (DNICs) [(NO)2Fe(SR)2]– (R = Et, Ph) into [4Fe-4S] Clusters [Fe4S4(SPh)4]2–“. Thesis, 2009. http://ndltd.ncl.edu.tw/handle/43834688213528712968.
Der volle Inhalt der QuelleMaerker, Claudia [Verfasser]. „Die zwei metabolischen Funktionen der Aconitase AcoA aus Aspergillus nidulans : Aconitase-Aktivität im (4Fe-4S)2+ und Methylisocitrat-Dehydratase-Aktivität im (3Fe-4S)+-Zustand / von Claudia Maerker“. 2007. http://d-nb.info/98410786X/34.
Der volle Inhalt der QuelleRomano, Christine Anne. „DNA-Mediated Charge Transfer Between [4Fe-4S] Cluster Glycosylases“. Thesis, 2011. https://thesis.library.caltech.edu/6277/2/Chapter_2.pdf.
Der volle Inhalt der QuelleThe work performed herein describes three proteins: Uracil DNA glycosylase (UDG) from Archaeoglobus fulgidus, MutY, and Endonuclease III (EndoIII) from Escherichia coli. They are DNA repair glycosylases that contain [4Fe-4S] clusters. While the catalytic mechanisms of many BER enzymes have been studied in detail, questions remain about how these enzymes search the vast amount of cellular DNA to find their substrates, and why some require a [4Fe-4S] cluster. The iron-sulfur cluster is not necessary for catalysis, and it only displays a physiologically relevant midpoint potential when bound to DNA. We have proposed that UDG, MutY, and EndoIII use their [4Fe-4S] clusters to participate in DNA-mediated charge transport (CT), and that these proteins mediate long-range electrochemical signaling in order to detect DNA damage.
This scheme for DNA damage detection assumes that CT occurs efficiently between the DNA helix and the [4Fe-4S] cluster of the bound protein. In order for efficient CT to occur, a pathway of amino acids must be present that facilitates CT between the DNA and the iron-sulfur cluster. For each of the enzymes mentioned, this pathway was explored through mutagenesis. In UDG, MutY, and EndoIII, several amino acids thought to be important for CT were mutated and the resulting proteins were characterized biochemically. Their CT capabilities were analyzed by cyclic voltammetry on DNA-modified electrodes. In these experiments, the mutants’ signal intensities were quantified and compared to those of wild-type enzyme. An attenuated signal relative to wild-type protein may indicate that the mutant is deficient in CT and that the targeted amino acid is part of the protein-DNA CT pathway in the native enzyme. Many mutants were also screened by enzymatic assays and circular dichroism spectroscopy to further characterize their DNA-binding properties and structural stability.
The A. fulgidus UDG mutants examined, C17H, C85S, and C101S, all contained mutations in the cysteine residues that ligate the [4Fe-4S] cluster. These mutants were designed to determine how the iron-sulfur cluster coordination environment affects protein-DNA CT. The mutants exhibited varying signal strengths relative to WT UDG on DNA-modified electrodes. C85S produced a weaker signal, indicating a CT deficiency. The signal intensity from C101S was within error of that of WT, and the signal from C17H was larger than that of WT, possibly indicating that this mutant is less structurally stable than WT UDG.
In E. coli MutY, position Y82 aligns with Y165 in MUTYH, a residue in which mutations have been found in many colorectal cancer patients. To better understand the correlation between protein-DNA CT and colorectal cancer, the MutY mutants Y82C and Y82L were prepared and characterized. Y82C exhibited a CT deficiency relative to WT MutY, whereas Y82L did not. These data indicate that Y82 forms part of the CT pathway in native E. coli MutY, but that other long-chain amino acids, such as leucine, can also mediate CT efficiently at this position.
Several different mutants of E. coli EndoIII were examined. First, the Y82 position was targeted, since the aligning MUTYH residue has been found mutated in colorectal cancer patients and because this residue is located near the protein-DNA interface. Five mutations were made at or near the Y82 position, and their cyclic voltammetry signals demonstrated that aromatic amino acids best mediate CT at this position. Other residues towards the interior of the protein, Y75, Y55, and F30 were also mutated to alanines. These mutants exhibited CT deficiencies, implicating the residues as part of a potential CT pathway. Residues W178 and Y185, located near the [4Fe-4S] cluster of EndoIII, were also mutated to alanines. The resulting mutants produced larger signals than that of WT EndoIII. These mutants were later shown by circular dichroism spectroscopy to be less stable structurally than WT EndoIII. All of the mutants mentioned exhibited enzymatic properties similar to those of WT, suggesting that they are able to bind DNA and excise damage nucleobases as well as the native enzyme. Several of these mutants were also used in a mutagenesis-based experiment to assay how EndoIII variants help MutY search for DNA lesions, although data from these experiments showed no significant differences in mutation rate between strains expressing different EndoIII variants.
In total, the mutagenesis studies performed here helped determine the characteristics of BER enzymes that enable them to mediate DNA-protein CT. All these enzymes must contain a stable, well-protected metallocluster that charge can access through a series of CT-facilitating amino acids. In discovering several residues important for protein-DNA CT in UDG, MutY, and EndoIII, we have strengthened support for the hypothesis that these enzymes facilitate DNA-mediated CT in vivo. These enzymes may in fact be part of a much larger array of redox-active DNA-binding proteins that communicate electrochemically to help each other detect and repair DNA lesions inside the cell.
Buchteile zum Thema "[4Fe-4S]2+"
Bethanis, Kostas, Petros Giastas, Trias Thireou und Vassilis Atlamazoglou. „Macromolecular Crystallographic Computing“. In Biocomputation and Biomedical Informatics, 1–36. IGI Global, 2010. http://dx.doi.org/10.4018/978-1-60566-768-3.ch001.
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