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Relevant bibliographies by topics / Iron sulphur proteins

Academic literature on the topic 'Iron sulphur proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 27 January 2023

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Journal articles on the topic "Iron sulphur proteins"

1

DING, Huangen, and Robert J. CLARK. "Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein." Biochemical Journal 379, no. 2 (April 15, 2004): 433–40. http://dx.doi.org/10.1042/bj20031702.

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Iron–sulphur clusters are one of the most common types of redox centre in biology. At least six proteins (IscS, IscU, IscA, HscB, HscA and ferredoxin) have been identified as being essential for the biogenesis of iron–sulphur proteins in bacteria. It has been shown that IscS is a cysteine desulphurase that provides sulphur for iron–sulphur clusters, and that IscU is a scaffold for the IscS-mediated assembly of iron–sulphur clusters. The iron donor for iron–sulphur clusters, however, remains elusive. Here we show that IscA is an iron binding protein with an apparent iron association constant of 3.0×1019 M−1, and that iron-loaded IscA can provide iron for the assembly of transient iron–sulphur clusters in IscU in the presence of IscS and l-cysteine in vitro. The results suggest that IscA is capable of recruiting intracellular iron and delivering iron for iron–sulphur clusters in proteins.

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2

Lill, Roland. "Function and biogenesis of iron–sulphur proteins." Nature 460, no. 7257 (August 2009): 831–38. http://dx.doi.org/10.1038/nature08301.

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3

Seidler, A., K. Jaschkowitz, and M. Wollenberg. "Incorporation of iron-sulphur clusters in membrane-bound proteins." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 418–21. http://dx.doi.org/10.1042/bst0290418.

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The completely sequenced genome of the cyano-bacterium Synechocystis PCC 6803 contains several open reading frames, of which the deduced amino acid sequences show similarities to proteins known to be involved in FeS cluster synthesis of nitrogenase (Nif proteins) and other FeS proteins (Isc proteins). In this article, the results of our studies on these proteins are summarized and discussed with respect to their relevance in FeS cluster incorporation in chloroplasts. In cyanobacteria, there appears to exist several pathways for FeS cluster synthesis.

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Seidler, A., K. Jaschkowitz, and M. Wollenberg. "Incorporation of iron-sulphur clusters into membrane-bound proteins." Biochemical Society Transactions 29, no. 3 (June 1, 2001): A51. http://dx.doi.org/10.1042/bst029a051a.

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5

Goldberg, Alina V., Sabine Molik, Anastasios D. Tsaousis, Karina Neumann, Grit Kuhnke, Frederic Delbac, Christian P. Vivares, Robert P. Hirt, Roland Lill, and T. Martin Embley. "Localization and functionality of microsporidian iron–sulphur cluster assembly proteins." Nature 452, no. 7187 (March 2, 2008): 624–28. http://dx.doi.org/10.1038/nature06606.

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Rouault, Tracey A. "Mammalian iron–sulphur proteins: novel insights into biogenesis and function." Nature Reviews Molecular Cell Biology 16, no. 1 (November 26, 2014): 45–55. http://dx.doi.org/10.1038/nrm3909.

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7

Sundararajan, M., J. P. McNamara, M. Mohr, I. H. Hillier, and H. Wang. "A semi-empirical molecular orbital scheme to study electron transfer in iron–sulphur proteins." Biochemical Society Transactions 33, no. 1 (February 1, 2005): 20–21. http://dx.doi.org/10.1042/bst0330020.

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We describe the use of the semi-empirical molecular orbital method PM3 (parametric method 3) to study the electronic structure of iron–sulphur proteins. We first develop appropriate parameters to describe models of the redox site of rubredoxins, followed by some preliminary calculations of multinuclear iron systems of relevance to hydrogenases.

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8

Frazzon, J., J. R. Fick, and D. R. Dean. "Biosynthesis of iron-sulphur clusters is a complex and highly conserved process." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 680–85. http://dx.doi.org/10.1042/bst0300680.

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Iron-sulphur ([Fe-S]) clusters are simple inorganic prosthetic groups that are contained in a variety of proteins having functions related to electron transfer, gene regulation, environmental sensing and substrate activation. In spite of their simple structures, biological [Fe-S] clusters are not formed spontaneously. Rather, a consortium of highly conserved proteins is required for both the formation of [Fe-S] clusters and their insertion into various protein partners. Among the [Fe-S] cluster biosynthetic proteins are included a pyridoxal phosphate-dependent enzyme (NifS) that is involved in the activation of sulphur from L-cysteine, and a molecular scaffold protein (NifU) upon which [Fe-S] cluster precursors are formed. The formation or transfer of [Fe-S] clusters appears to require an electron-transfer step. Another complexity is that molecular chaperones homologous to DnaJ and DnaK are involved in some aspect of the maturation of [Fe-S]-cluster-containing proteins. It appears that the basic biochemical features of [Fe-S] cluster formation are strongly conserved in Nature, since organisms from all three life Kingdoms contain the same consortium of homologous proteins required for [Fe-S] cluster formation that were discovered in the eubacteria.

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9

Armstrong, Fraser A. "Voltammetric studies of the reactions of iron-sulphur centers in proteins." Journal of Inorganic Biochemistry 43, no. 2-3 (August 1991): 238. http://dx.doi.org/10.1016/0162-0134(91)84228-2.

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10

Degli Esposti, M., F. Ballester, G. Solaini, and G. Lenaz. "The circular-dichroic properties of the ‘Rieske’ iron-sulphur protein in the mitochondrial ubiquinol: cytochrome c reductase." Biochemical Journal 241, no. 1 (January 1, 1987): 285–90. http://dx.doi.org/10.1042/bj2410285.

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We have studied the c.d. spectra of the ‘Rieske’ iron-sulphur protein isolated from the ubiquinol: cytochrome c reductase (bc1 complex) of bovine heart mitochondria. Both the oxidized and the reduced form of the ‘Rieske’ protein display a series of well-resolved c.d. features resembling those reported for the ‘Rieske’-type iron-sulphur protein purified from the bacterium Thermus thermophilus [Fee, Findling, Yoshida, Hille, Tarr, Hearshen, Dunham, Day, Kent & Münck (1984) J. Biol, Chem. 259, 124-133]. In particular, the difference spectra, reduced minus oxidized, of both proteins have a distinctive negative band at 497 nm. The c.d. features characteristic of the isolated ‘Rieske’ protein were found in the dichroic spectra of the whole bc1 complex in the region between 450 and 520 nm. The reduction of the enzyme by ascorbate or ubiquinol is accompanied by the formation of a negative band at about 500 nm that corresponds, in all its c.d. properties, to the specific dichroic absorption of the reduced ‘Rieske’ iron-sulphur protein.

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Dissertations / Theses on the topic "Iron sulphur proteins"

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

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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3

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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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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5

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 response to changes in the levels of cytosolic 5,10-CH2-H??4folate (Piper et al., 2000). Given the centrality of 5,10-CH2-H??4folate to many aspects of metabolism, it was hypothesised that other genes may be regulated by the same mechanism. Using microarray analysis of S. cerevisiae under a number of conditions that affect 5,10-CH2-H??4folate levels, the ??one-carbon regulon??, a group of genes that were co-regulated with the GCV genes was identified. The one-carbon regulon corresponds closely to genes whose promoters are bound by the purine biosynthesis regulator Bas1p, but not all one-carbon regulon members are significantly purine regulated. Genetic approaches demonstrated that the one-carbon unit response and the purine response are distinct, though both depend on the presence of Bas1p. This demonstrated that the close metabolic connections of one-carbon and purine metabolism are reflected in over-lapping, but separable regulatory mechanisms. The identity of the sensor of one-carbon unit depletion remains unknown, but in the course of investigation of the candidate regulator Caf17p, it was demonstrated that Caf17p is in fact involved in Fe/S cluster protein maturation. Examination of the effects of Caf17p depletion revealed that Caf17p is required for the function and maturation of the related mitochondrial Fe/S proteins aconitase and homoaconitase, as well as the function of, but not de novo iron incorporation into, the mitochondrial radical-SAM Fe/S protein biotin synthase. Because other Fe/S proteins were unaffected, Caf17p appears to be a specialised Fe/S maturation factor. The presence of a putative H4folate binding site indicates that Caf17p may constitute a metabolic link between one-carbon and iron metabolism.

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6

Rudolf, Jana. "Characterisation of XPD from Sulfolobus acidocaldarius : an iron-sulphur cluster containing DNA repair helicase." Thesis, St Andrews, 2007. http://hdl.handle.net/10023/159.

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7

Filenko, Nina. "Roles and regulation of the iron-sulphur proteins, HCP, NapG and NapH, induced during anaerobic growth of E. coli." Thesis, University of Birmingham, 2005. http://etheses.bham.ac.uk//id/eprint/8706/.

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The periplasmic nitrate reductase (Nap) has been shown to support anaerobic growth of Escherichia coli K-12 under nitrate-limiting conditions. Two of the Nap proteins, NapG and NapH, are predicted to contain four and two [4Fe-4S] clusters, respectively. In this thesis it is reported that, during fermentative growth. Nap plays a role in redox balancing. This role is most pronounced in a strain that lacks menaquinol and tiierefore cannot use the menaquinol-dependent ftunarate reductase to fulfil a redox balancing role during glucose fermentation. Nitrate stimulated the growth of both a AmenBC AnapGH and an isogenic AmenBC nap^ strain to the same extent, even although the Nap activity was extremely low. This showed that the residual 1% electron flow in the strain deleted for NapG and NapH was sufficient to fulfil this redox balancing function. Using artificial quinones, NapG and NapH were shown to be linked to oxidation of quinones with high midpoint redox potentials. NapF^ and NapF' strains were grown anaerobically after either aerobic or anaerobic growth and NapF was shown to be involved in adaptation from aerobic to anaerobic growth. The hybrid cluster protein (HCP) contains two Fe-S clusters, one of which is a hybrid [4Fe-2S-20] cluster. Despite intensive study, its physiological function is unclear. E. coli HCP is detected after anaerobic growth with nitrate or nitrite, so a possible role for it in some stage of the nitrogen cycle has been proposed. To study the regulation of HCP, an hcprlacZ fusion was constructed and transformed into_^r, arcA and norR mutant strains of E. coli. Transcription from the hep promoter was induced during anaerobic growth. Only the jhr mutant was defective in hep expression, suggesting that transcription from the promoter in response to anaerobiosis is dependent on FNR. Nitrate and nitrite fiirther induced transcription from the hep promoter. The parental strain and the narL, narP and narLmrP mutants were grown anaerobically in medium supplemented with nitrite or nitrate. The nitrite and nitrate response of the hep promoter was mediated by both of the response regulator proteins, NarL and NarP. It is argued that NarL plays a dual role at the hep promoter acting as an activator during growth in the presence of a low concentration of nitrite or nitrate and as both repressor and activator in the presence of high nitrite or nitrate concentrations. Gel retardation assays were used to show that FNR and NarL form a complex with the hep promoter, thus confirming that their effect on transcription is direct. A technique involving the rapid amplification of cDNA ends (RACE) was used to demonstrate that transcription of the hcp~hcr operon initiates at a thymine nucleotide located 31 bp upstream of the translation-initiation codon. A A/icp strain was constructed by homologous recombination. When grown in medium supplemented with nitrate, the growth rate and yield of the parental strain and the hhep mutant were the same, suggesting that HCP is not involved in nitrate-dependent growth. Both HCP^ and HCP' strains were equally sensitive to nitric oxide and hydroxylamine. It was concluded therefore that HCP is unable to protect bacteria against nitric oxide or hydroxylamine toxicity in vivo. HCP was overexpressed from a recombinant plasmid and subsequently purified on a nickel column for biochemical studies. A qualitative method using reduced methyl viologen as an electron donor was developed for use in attempts to identify a possible substrate of HCP in vitro. Nitrite, nitrate and hydroxylamine were tested, but no evidence was presented that any of them can be used as an electron acceptor.

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8

Alhebshi, Alawiah. "The essential iron-sulphur protein Rli1 is a key determinant of oxidative stress resistance in Saccharomyces cerevisiae." Thesis, University of Nottingham, 2014. http://eprints.nottingham.ac.uk/13974/.

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Reactive oxygen species (ROS) are linked to a range of degenerative conditions in humans, and may cause damage to an array of cellular components. However, it is unclear which cellular target(s) of ROS may primarily account for toxicity during oxidative stress. The sensitivity of iron-sulphur (Fe-S) clusters to ROS makes these candidate determinants of ROS mediated cell killing. Ribonuclease L inhibitor (Rli1p) is a highly conserved protein that is essential in all tested eukaryotes and archaea, but requires Fe-S clusters for its crucial functions in protein synthesis. Herein, the novel hypothesis that ROS toxicity is caused by loss of Rli1p function was tested. Rli1p activity (in nuclear export of ribosomal subunits) was impaired during mild oxidative stress in yeast. In addition, resistance to pro-oxidants was decreased by RLI1 repression and increased by RLI1 overexpression. This Rli1p-dependency was abolished during anaerobicity and accentuated in cells expressing the Fe-S cluster defective Rli1p construct, rli1C58A. The effects appeared specific to Rli1p as overexpression of other essential Fe-S proteins did not increase stress resistance. Methionine sulphoxide reductases (MSRs) and the Mn-superoxide dismutase (Sod2p) are known to help preserve the integrity of Fe-S clusters in cells. Here, these proteins’ antioxidant actions were shown to be at least partly mediated through Rli1p. Resistance to both chronic and acute oxidative stress was Rli1p-dependent. Further experiments indicated that Rli1p-dependent protein synthesis could be a critical target of ROS and, specifically, that Rli1p function may help to protect against ROS-induced mRNA mistranslation. The study indicated that Rli1p function is a primary biological target of ROS action, owing to its essential nature but dependency on ROS-labile Fe-S clusters. Such insights could offer new approaches for combating oxidative stress-related disease.

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9

Knight, Julie Sylvia. "The isolation, characterization and expression of the gene encoding the chloroplast Rieske iron-sulphur protein of Arabidopsis thaliana." Thesis, University of Cambridge, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338309.

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10

Soares, Cindy Nunes. "Isolation and Characterization of Novel Iron-Sulphur Proteins from DvH Involved in Cell Division." Master's thesis, 2016. http://hdl.handle.net/10362/61272.

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Firstly, isolated from Desulfovibrio gigas, the Orange Protein presents a unique type of mixed metal sulphur cluster composed by two different metals, molybdenum and copper. This protein forms a complex with other proteins, that has recently been proposed to be involved in anaerobic cell division of D. vulgaris Hildenborough. In this Master thesis, DVU2103 ATPase from D. vulgaris Hildenborough was purified and biochemically characterized. Since the metal cluster present in this protein has been proven to be oxygen sensitive, the purification was performed under anoxic environment. The protein was co-purified with other proteins of the orp operon, DVU2108 and possibly DVU2104, as a protein complex (heterotrimer) confirming that this complex has physiological meaning. The protein complex was purified with an average yield of 58 ± 28 μg, and presents 5.3 ± 0.3 Fe atoms/Total protein. DVU2103 complex presents a broad absorption band at 400 nm in its visible spectrum characteristic of [4Fe-4S] clusters and ICP-AES analysis confirm the presence of either one or two [4Fe4S] clusters. As-isolated protein is mainly EPR active presenting a rhombic signal, with g values of 2.06, 1.89 and 1.85, that switches to an axial signal when reduced with dithionite. Dithionite, unlike ascorbate, is responsible for the full reduction of the metallic centre. Studies to determine the apparent molecular mass of the complex revealed that ATP affects its conformational structure, making it more compact, and oxic conditions lead to the destruction of the [Fe-S] cluster, with concomitant formation of a larger oligomer. ATPase activity of “DVU2103” complex was tested under anoxic and oxic conditions, showing that the protein has a higher activity under the former. Considering that the exposure to oxygen leads to the destruction of the [Fe-S] cluster, it can be concluded that it is essential for higher activity. In this thesis the homologous expression and purification of DVU2108 in D. vulgaris Hildenborough was also performed. No Mo/Cu heterometallic cluster was detected in this protein after purification under anoxic conditions, nevertheless Fe/protein ratio of 1 was estimated for this sample.

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Books on the topic "Iron sulphur proteins"

1

Cammack, Richard. Iron-Sulfur Proteins. Burlington: Elsevier, 1999.

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2

Ōae, Shigeru. Organic sulfur chemistry: Structure and mechanism. Edited by Doi Joyce Takahashi. Boca Raton, Fla: CRC Press, 1991.

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3

George, Simon Justin. Magnetic circular dichromism studies of iron-sulpher proteins. Norwich: University of East Anglia, 1986.

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Sykes, A. G., and Richard Cammack. Advances in Inorganic Chemistry: Iron-Sulphur Proteins (Advances in Inorganic Chemistry). Academic Press, 1992.

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Oae, Shigeru, and Tadashi Okuyama. Organic Sulfur Chemistry: Biochemical Aspects. CRC, 1992.

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Oae, Shigeru. Organic Sulfur Chemistry. Taylor & Francis Group, 2018.

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Organic Sulfur Chemistry. Taylor & Francis Group, 2017.

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Shigeru, Ōae, and Okuyama Tadashi 1956-, eds. Organic sulfur chemistry. Boca Raton, Fla: CRC Press, 1992.

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Oae, Shigeru. Organic Sulfur Chemistry. Taylor & Francis Group, 2018.

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Oae, Shigeru. Organic Sulfur Chemistry. Taylor & Francis Group, 2018.

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Book chapters on the topic "Iron sulphur proteins"

1

Thomson, A. J. "Iron-Sulphur Proteins." In Metalloproteins, 79–120. London: Palgrave Macmillan UK, 1985. http://dx.doi.org/10.1007/978-1-349-06372-7_3.

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Gari, Kerstin. "13 Iron-sulphur proteins and genome stability." In Biochemistry, Biosynthesis and Human Diseases, edited by Tracey Rouault. Berlin, Boston: De Gruyter, 2017. http://dx.doi.org/10.1515/9783110479850-013.

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Maynard Smith, John, and Eors Szathmary. "The origin of protocells." In The Major Transitions in Evolution. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780198502944.003.0011.

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Cellularization has the following main aspects that we have to explain: • The need for active (self-generated) compartmentation when metabolism is liberated from the surface. • The origin of membranogenic molecules and membranes. • The origin and mechanism of spontaneous protocell fission. • The transportation problem. Simple membranes are not ‘leaky’ enough to permit important nutrients to pass through. • Were the first protocells autotrophs or heterotrophs? The evolution of the first autocatalytic metabolic cycle. • The iron-sulphur world and the RNA world: are they mutually exclusive or complementary? • The problem of the origin of the two membranes of negibacteria, the most ancient existing group of organisms. • The origin of chromosomes and DNA synthesis. We shall discuss these problems in turn. As we discussed before, the prebiotic pizza has the ability to localize metabolites and genes. This is advantageous for two reasons: Reactants are kept in each other’s proximity, which ensures that reaction rates will be high enough and that important compounds do not drift away. Genes will interact, directly (e.g. by influencing each other’s replication) or indirectly (by catalysing steps of metabolism), only with their neighbours: selection will thus be able to ensure cooperation among genes that would otherwise compete against each other. Life liberated itself from surfaces a long time ago. Somehow, passive localization must have been replaced by an active process of membrane generation, maintenance and fission. The basic structure of contemporary biomembranes is as follows. There is a molecular bilayer of lipids, to which proteins are attached in various ways. The bilayer is formed because the membrane constituents are so-called amphipathic molecules: they have a hydrophilic head and a hydrophobic tail. Since the binding interaction of water with itself is much stronger than that between water and hydrophobic compounds, the latter are expelled by water as much as possible; this results in tails coming together. A simple sheet of bilayer would still be not at the energy minimum because its edges would be exposed to water. An energetically favourable solution is the formation of a lipid vesicle.

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