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On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes [PDF]
Iron and sulfur are indispensable elements of every living cell, but on their own these elements are toxic and require dedicated machineries for the formation of iron/sulfur (Fe/S) clusters. In eukaryotes, proteins requiring Fe/S clusters (Fe/S proteins) are found in or associated with various organelles including the mitochondrion, endoplasmic ...
Anastasios Tsaousis +1 more
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Iron–sulfur cluster biosynthesis [PDF]
Iron–sulfur (Fe–S) clusters are present in more than 200 different types of enzymes or proteins and constitute one of the most ancient, ubiquitous and structurally diverse classes of biological prosthetic groups. Hence the process of Fe–S cluster biosynthesis is essential to almost all forms of life and is remarkably conserved in prokaryotic and ...
Sibali, Bandyopadhyay +2 more
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Erythropoiesis and Iron Sulfur Cluster Biogenesis [PDF]
Erythropoiesis in animals is a synchronized process of erythroid cell differentiation that depends on successful acquisition of iron. Heme synthesis depends on iron through its dependence on iron sulfur (Fe-S) cluster biogenesis. Here, we review the relationship between Fe-S biogenesis and heme synthesis in erythropoiesis, with emphasis on the proteins,
Hong Ye, Tracey A. Rouault
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Spectral decomposition of iron-sulfur clusters
The near universal availability of UV-Visible spectrophotometers makes this instrument a highly exploited tool for the inexpensive, rapid examination of iron-sulfur clusters. Yet, the analysis of iron-sulfur cluster reconstitution experiments by UV-Vis spectroscopy is notoriously difficult due to the presence of broad, ill-defined peaks. Other types of
Isaiah O. Betinol +2 more
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Lights on Iron-Sulfur Clusters
The biogenesis of iron-sulfur proteins within a living cell is traditionally investigated by enzyme activity measurements and radiolabeling techniques. In this issue of Chemistry and Biology, Hoff et al. introduce a non-invasive fluorescence-based method to trace the formation of iron-sulfur clusters at high sensitivity.
Lillig, C., Lill, R.
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Redox-Sensing Iron–Sulfur Cluster Regulators [PDF]
Significance: Iron–sulfur cluster proteins carry out multiple functions, including as regulators of gene transcription/translation in response to environmental stimuli. In all known cases, the cluster acts as the sensory module, where the inherent reactivity/fragility of iron–sulfur clusters with small/redox ...
Crack, Jason C., Le Brun, Nick E.
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Modelling the Hydrolysis of Iron-Sulfur Clusters
Iron-sulfur (FeS) clusters are essential metal cofactors involved in a wide variety of biological functions. Their catalytic efficiency, biosynthesis and regulation depend on FeS stability in aqueous solution. Here, molecular modelling is used to investigate the hydrolysis of an oxidized (ferric) mononuclear FeS cluster by bare dissociation and water ...
Murilo H. Teixeira +6 more
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The role of chaperones in iron–sulfur cluster biogenesis [PDF]
Iron–sulfur cluster biogenesis is a complex process mediated by numerous proteins among which two from bacteria chaperones, called HscB and HscA in bacteria. They are highly conserved up to eukaryotes and homologous to DnaJ and DnaK, respectively, but with specific differences. As compared with other chaperones, HscB and HscA have escaped attention and
Puglisi, Rita, Pastore, Annalisa
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Hybrid Methods in Iron-Sulfur Cluster Biogenesis [PDF]
Hybrid methods, which combine and integrate several biochemical and biophysical techniques, have rapidly caught up in the last twenty years to provide a way to obtain a fuller description of proteins and molecular complexes with sizes and complexity otherwise not easily affordable.
Prischi, Filippo, Pastore, Annalisa
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The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster.
It has been reported (Ruzicka, F.J., and Beinert, H. (1978) J. Biol. Chem. 253, 2514-2517) that aconitase in the oxidized state, as isolated, shows an electron paramagnetic resonance signal centered at g = 2.01, typical of high potential iron-sulfur proteins.
D M, Kurtz +5 more
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