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Relevant bibliographies by topics / [4Fe-4S]2+

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Academic literature on the topic '[4Fe-4S]2+'

Author: Grafiati

Published: 20 July 2024

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Journal articles on the topic "[4Fe-4S]2+"

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Azam, Tamanna, Jonathan Przybyla-Toscano, Florence Vignols, Jérémy Couturier, Nicolas Rouhier, and Michael K. Johnson. "[4Fe-4S] cluster trafficking mediated by Arabidopsis mitochondrial ISCA and NFU proteins." Journal of Biological Chemistry 295, no. 52 (2020): 18367–78. http://dx.doi.org/10.1074/jbc.ra120.015726.

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Numerous iron-sulfur (Fe-S) proteins with diverse functions are present in the matrix and respiratory chain complexes of mitochondria. Although [4Fe-4S] clusters are the most common type of Fe-S cluster in mitochondria, the molecular mechanism of [4Fe-4S] cluster assembly and insertion into target proteins by the mitochondrial iron-sulfur cluster (ISC) maturation system is not well-understood. Here we report a detailed characterization of two late-acting Fe-S cluster-carrier proteins from Arabidopsis thaliana, NFU4 and NFU5. Yeast two-hybrid and bimolecular fluorescence complementation studies

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Duan, Xuewu, Juanjuan Yang, Binbin Ren, Guoqiang Tan, and Huangen Ding. "Reactivity of nitric oxide with the [4Fe–4S] cluster of dihydroxyacid dehydratase from Escherichia coli." Biochemical Journal 417, no. 3 (2009): 783–89. http://dx.doi.org/10.1042/bj20081423.

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Although the NO (nitric oxide)-mediated modification of iron–sulfur proteins has been well-documented in bacteria and mammalian cells, specific reactivity of NO with iron–sulfur proteins still remains elusive. In the present study, we report the first kinetic characterization of the reaction between NO and iron–sulfur clusters in protein using the Escherichia coli IlvD (dihydroxyacid dehydratase) [4Fe–4S] cluster as an example. Combining a sensitive NO electrode with EPR (electron paramagnetic resonance) spectroscopy and an enzyme activity assay, we demonstrate that NO is rapidly consumed by t

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Sutton, Victoria R., Erin L. Mettert, Helmut Beinert, and 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, no. 23 (2004): 8018–25. http://dx.doi.org/10.1128/jb.186.23.8018-8025.2004.

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ABSTRACT The ability of FNR to sense and respond to cellular O2 levels depends on its [4Fe-4S]2+ cluster. In the presence of O2, the [4Fe-4S]2+ cluster is converted to a [2Fe-2S]2+ cluster, which inactivates FNR as a transcriptional regulator. In this study, we demonstrate that ∼2 Fe2+ ions are released from the reaction of O2 with the [4Fe-4S]2+ cluster. Fe2+ release was then used as an assay of reaction progress to investigate the rate of [4Fe-4S]2+ to [2Fe-2S]2+ cluster conversion in vitro. We also found that there was no detectable difference in the rate of O2-induced cluster conversion fo

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George, S. J., F. A. Armstrong, E. C. Hatchikian, and 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, no. 1 (1989): 275–84. http://dx.doi.org/10.1042/bj2640275.

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Desulfovibrio africanus ferredoxin III is a protein (Mr 6585) containing one [3Fe-4S]1+,0 and one [4Fe-4S]2+,1+ core cluster when aerobically isolated. The amino acid sequence contains only seven cysteine residues, the minimum required to ligand these two clusters. Cyclic voltammery by means of direct electrochemistry at a pyrolytic-graphite-‘edge’ electrode promoted by neomycin shows that, when reduced, the [3Fe-4S]0 centre reacts rapidly with Fe(II) ion to form a [4Fe-4S]2+ cluster. The latter, which can be reduced at a redox potential similar to that of the other [4Fe-4S] cluster, must incl

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Azam, Tamanna, Jonathan Przybyla-Toscano, Florence Vignols, Jérémy Couturier, Nicolas Rouhier, and 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, no. 23 (2020): 9237. http://dx.doi.org/10.3390/ijms21239237.

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Iron-sulfur (Fe-S) proteins are crucial for many cellular functions, particularly those involving electron transfer and metabolic reactions. An essential monothiol glutaredoxin GRXS15 plays a key role in the maturation of plant mitochondrial Fe-S proteins. However, its specific molecular function is not clear, and may be different from that of the better characterized yeast and human orthologs, based on known properties. Hence, we report here a detailed characterization of the interactions between Arabidopsis thaliana GRXS15 and ISCA proteins using both in vivo and in vitro approaches. Yeast t

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Dridge, Elizabeth J., Carys A. Watts, Brian J. N. Jepson, et al. "Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy." Biochemical Journal 408, no. 1 (2007): 19–28. http://dx.doi.org/10.1042/bj20070669.

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Periplasmic SER (selenate reductase) from Thauera selenatis is classified as a member of the Tat (twin-arginine translocase)-translocated (Type II) molybdoenzymes and comprises three subunits each containing redox cofactors. Variable-temperature X-band EPR spectra of the purified SER complex showed features attributable to centres [3Fe–4S]1+, [4Fe–4S]1+, Mo(V) and haem-b. EPR-monitored redox-potentiometric titration of the SerABC complex (SerA–SerB–SerC, a hetero-trimetric complex of αβγ subunits) revealed that the [3Fe–4S] cluster (FS4, iron-sulfur cluster 4) titrated as n=1 Nernstian compone

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BUSCH, Johanneke L. H., Jacques L. BRETON, Barry M. BARTLETT, Fraser A. ARMSTRONG, Richard JAMES, and Andrew J. THOMSON. "[3Fe-4S]↔[4Fe-4S] cluster interconversion in Desulfovibrio africanus ferredoxin III: properties of an Asp14→Cys mutant." Biochemical Journal 323, no. 1 (1997): 95–102. http://dx.doi.org/10.1042/bj3230095.

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The 8Fe ferredoxin III from Desulfovibrio africanus is a monomeric protein which contains two [4Fe-4S]2+/1+ clusters, one of which is labile and can readily and reversibly lose one Fe under oxidative conditions to yield a [3Fe-4S]1+/0 cluster. This 4Fe cluster has an S = 3/2 ground spin state instead of S = 1/2 in the reduced +1 state [George, Armstrong, Hatchikian and Thomson (1989) Biochem. J.264, 275-284]. The co-ordination to this cluster is unusual in that an aspartate (Asp14, D14) is found where a cysteine residue normally occurs. Using a mutant protein obtained from the overexpression i

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Smith, Eugene T., Dennis W. Bennett, and Benjamin A. Feinberg. "Redox properties of 2[4Fe4S] ferredoxins." Analytica Chimica Acta 251, no. 1-2 (1991): 27–33. http://dx.doi.org/10.1016/0003-2670(91)87111-j.

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Roland, Mélanie, Jonathan Przybyla-Toscano, Florence Vignols, et al. "The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins." Journal of Biological Chemistry 295, no. 6 (2020): 1727–42. http://dx.doi.org/10.1074/jbc.ra119.011034.

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Proteins incorporating iron–sulfur (Fe-S) co-factors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries in plants, located in the cytosol, mitochondria, and chloroplasts. After de novo formation on scaffold proteins, transfer proteins load Fe-S clusters onto client proteins. Among the plastidial representatives of these transfer proteins, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters present in photosystem I subunits, acting upstream of the high-chlorophyll fluorescence 101 (HCF101) protein. NFU2 is a

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Stripp, Sven T., Jonathan Oltmanns, Christina S. Müller, et al. "Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly." Biochemical Journal 478, no. 17 (2021): 3281–95. http://dx.doi.org/10.1042/bcj20210224.

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The [4Fe-4S] cluster containing scaffold complex HypCD is the central construction site for the assembly of the [Fe](CN)2CO cofactor precursor of [NiFe]-hydrogenase. While the importance of the HypCD complex is well established, not much is known about the mechanism by which the CN− and CO ligands are transferred and attached to the iron ion. We report an efficient expression and purification system producing the HypCD complex from E. coli with complete metal content. This enabled in-depth spectroscopic characterizations. The results obtained by EPR and Mössbauer spectroscopy demonstrate that

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Dissertations / Theses on the topic "[4Fe-4S]2+"

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Davasse, Valérie. "Ingénierie de la ferredoxine 2[4Fe-4S] de Clostridium pasteurianum." Grenoble 1, 1993. http://www.theses.fr/1993GRE10135.

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La ferredoxine 24fe-4s de la bacterie anaerobie clostridium pasteurianum est une proteine de 55 acides amines au caractere acide. Ses deux centres 4fe-4s sont lies a la chaine polypeptidique par l'intermediaire de 8 residus cysteine. Elle tient un role central de transporteur d'electrons dans le metabolisme de clostridium pasteurianum. Un gene codant pour cette ferredoxine a ete entierement synthetise a partir de 18 oligonucleotides. L'expression de ce gene chez escherichia coli produit une proteine recombinante totalement identique a la ferredoxine native. Le remplacement modulaire de segment

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Lenormand-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.

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Cette these se situe dans le cadre des modelisations chimiques de proteines fer-soufre, plus particulierement les proteines fer-soufre a haut potentiel (hipip). L'objectif est de synthetiser des centres 4fe-4s dans les deux etats d'oxydation physiologiques 4fe-4s#2+ et 4fe-4s#3+ et de les caracteriser d'un point de vue physico-chimique. L'hypothese a partir de laquelle le sujet a ete aborde consiste a supposer qu'il est necessaire d'etablir une zone steriquement encombree et hydrophobe autour de l'agregat afin de proteger le centre 4fe-4s#3+ d'une degradation oxydante. Pratiquement, un tel env

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Maerker, 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.

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Chan, 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.

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Le Nicotinamide Adénine Dinucléotide (NAD) est un cofacteur clé du métabolisme cellulaire. Synthétisé à partir d'acide quinolinique (QA) chez tous les organismes vivants, la biosynthèse du QA diffère entre les eucaryotes et les procaryotes. Chez les eucaryotes, il est produit à partir de L-tryptophane alors que chez les procaryotes et les plantes, il est synthétisé par l'action concertée de deux enzymes: la L-aspartate oxydase (NadB) qui permet la formation d'iminoaspartate (IA) à partir de L-aspartate et la quinolinate synthase (NadA) qui permet la condensation de deux molécules, la dihydroxy

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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.

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Les centres fer-soufre sont des groupements metalliques presents dans une grande variete de proteines ou ils assurent des fonctions tres diverses. Depuis plus d'une vingtaine d'annees, la description de leurs proprietes a suscite une somme considerable de travaux, mais la comprehension de leur structure electronique se heurte a plusieurs difficultes liees a la presence d'etats de valence mixte fe i i et fe i i i et a leur delocalisation sur plusieurs sites fe. Dans ce contexte, nous avons entrepris une etude systematique des proprietes magnetiques des centres 4fe4s 2 + / 3 + presents dans la p

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Jobelius, 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.

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IspH est la dernière enzyme de la voie du méthylérythritol phosphate qui produit les deux précurseurs nécessaires à la biosynthèse de tous les isoprénoïdes. Cette métalloenzyme est essentielle à la survie de nombreux microorganismes dont des bactéries pathogènes et le parasite responsable du paludisme. Etant absente chez l’humain, IspH est une cible de choix pour le développement de nouveaux agents antimicrobiens. En utilisant une approche pluridisciplinaire combinant biologie moléculaire, enzymologie, spectroscopies Raman, Mössbauer et cristallographie, l’objectif de cette thèse était d’étudi

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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.

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Lin, Zong-Sian, and 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.

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Maerker, 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.

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Romano, Christine Anne. "DNA-Mediated Charge Transfer Between [4Fe-4S] Cluster Glycosylases." Thesis, 2011. https://thesis.library.caltech.edu/6277/2/Chapter_2.pdf.

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<p>The 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 boun

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Book chapters on the topic "[4Fe-4S]2+"

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Bethanis, Kostas, Petros Giastas, Trias Thireou, and Vassilis Atlamazoglou. "Macromolecular Crystallographic Computing." In Biocomputation and Biomedical Informatics. IGI Global, 2010. http://dx.doi.org/10.4018/978-1-60566-768-3.ch001.

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Structural genomics or structural proteomics can be defined as the quest to obtain the three-dimensional structures of all proteins. Single-crystal X-ray crystallography provides the most direct, accurate and in most of the cases the only way of forming images of macromolecules. Using crystallography, threedimensional images have been made of thousands of macromolecules, especially proteins and nucleic acids. These give detailed information about their activity, their mechanism for recognizing and binding substrates and effectors, and the conformational changes which they may undergo. This chapter presents the basic crystallographic procedure steps and a thorough survey of the computational software used most frequently by protein X-ray crystallographers. The determination of the structure of 2[4Fe-4S] ferredoxin from Escherichia coli. is examined as a case study of implementation of these steps and programs. Finally, some of the perspectives of the field of computational X-ray crystallography are noted showing the future developments in the ceaseless evolution of new methods and proliferation of new programs.

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