The structure of iron–sulfur proteins
Progress in Biophysics and Molecular Biology, 1998 Ferredoxins are a group of iron-sulfur proteins for which a wealth of structural and mutational data have recently become available. Previously unknown structures of ferredoxins which are adapted to halophilic, acidophilic or hyperthermophilic environments and new cysteine patterns for cluster ligation and non-cysteine cluster ligation have been ...
H, Sticht, P, Rösch
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On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes
Frontiers in Microbiology, 2019 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)
Anastasios D. Tsaousis
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Magnetochemistry, 2020 The study of cellular machineries responsible for the iron–sulfur (Fe–S) cluster biogenesis has led to the identification of a large number of proteins, whose importance for life is documented by an increasing number of diseases linked to them.
Mario Piccioli
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Puzzling subunits of mitochondrial cytochrome reductase [PDF]
, 1990 The ubiquinol-cytochrome c reductase complex, like the other proton-pumping respiratory complexes of mitochondria, is an assembly of many different subunits.
Bechmann +22 more
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The synthesis and characterization of new higher nuclearity arene-ruthenium-sulfur clusters : a thesis presented in partial fulfillment of the requirements for the degree of Master of Science in Chemistry at Massey University, New Zealand [PDF]
, 1999 This thesis describes a project investigating the synthesis and characterization of new higher nuclearity arene-ruthenium-sulfur clusters and arene-ruthenium-nitrogen complexes.
Guo, Libei
core
Differentiated, promoter-specific response of [4Fe-4S] NsrR DNA-binding to reaction with nitric oxide [PDF]
, 2016 NsrR is an iron-sulfur cluster protein that regulates the nitric oxide (NO) stress response of many bacteria. NsrR from Streptomyces coelicolor regulates its own expression and that of only two other genes, hmpA1 and hmpA2, which encode HmpA enzymes ...
Crack, Jason +5 more
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The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions
Frontiers in Plant Science, 2013 Many metabolic pathways and cellular processes occurring in most sub-cellular compartments depend on the functioning of iron-sulfur (Fe-S) proteins, whose cofactors are assembled through dedicated protein machineries.
Jérémy eCouturier +4 more
doaj +1 more source
Cytochromes and iron sulfur proteins in sulfur metabolism of phototrophic bacteria [PDF]
Dissimilatory sulfur metabolism in phototrophic sulfur bacteria provides the bacteria with electrons for photosynthetic electron transport chain and, with energy.
Fischer, U.
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UV-light-driven prebiotic synthesis of iron–sulfur clusters [PDF]
, 2017 Iron–sulfur clusters are ancient cofactors that play a fundamental role in metabolism and may have impacted the prebiotic chemistry that led to life.
Bonfio, Claudia +13 more
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Crystallization of Adenylylsulfate Reductase from Desulfovibrio gigas: A Strategy Based on Controlled Protein Oligomerization [PDF]
, 2011 Adenylylsulfate reductase (adenosine 5′-phosphosulfate reductase, APS reductase or APSR, E.C.1.8.99.2) catalyzes the conversion of APS to sulfite in dissimilatory sulfate reduction. APSR was isolated and purified directly from massive anaerobically grown
Chan, Sunney I. +9 more
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