Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate.
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Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1pMitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae.Structural, Mechanistic and Coordination Chemistry of Relevance to the Biosynthesis of Iron-Sulfur and Related Iron CofactorsIron-sulfur cluster biosynthesis.Three hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complexRole of conserved cysteines in mediating sulfur transfer from IscS to IscUThe role of zinc in the stability of the marginally stable IscU scaffold protein.Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis.Redox chemistry of the Schizosaccharomyces pombe ferredoxin electron-transfer domain and influence of Cys to Ser substitutionsControlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandiiTangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfuraseInvestigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution of Grx3/4 AND Dre2 proteinsIron chaperones for mitochondrial Fe-S cluster biosynthesis and ferritin iron storageGlutathione complexed Fe-S centers.Human ferredoxin-2 displays a unique conformational changeEscherichia coli FtnA acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stressSolution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscUFe-S cluster assembly pathways in bacteria.Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteinsDrosophila frataxin: an iron chaperone during cellular Fe-S cluster bioassembly.Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB.Iron-sulfur cluster biosynthesis: characterization of a molten globule domain in human NFU.Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery.Cancer-Related NEET Proteins Transfer 2Fe-2S Clusters to Anamorsin, a Protein Required for Cytosolic Iron-Sulfur Cluster Biogenesis.Iron-sulfur cluster exchange reactions mediated by the human Nfu protein.Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein.Understanding the molecular basis for multiple mitochondrial dysfunctions syndrome 1 (MMDS1): impact of a disease-causing Gly189Arg substitution on NFU1.Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxinA dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins.SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly.Iron-sulfur cluster biosynthesis: biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly.Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein.Cytosolic iron-sulfur cluster transfer-a proposed kinetic pathway for reconstitution of glutaredoxin 3.Mapping cellular Fe-S cluster uptake and exchange reactions - divergent pathways for iron-sulfur cluster delivery to human ferredoxins.Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.Analysis of NFU-1 metallocofactor binding-site substitutions-impacts on iron-sulfur cluster coordination and protein structure and function.Investigation of glutathione-derived electrostatic and hydrogen-bonding interactions and their role in defining Grx5 [2Fe-2S] cluster optical spectra and transfer chemistry.Regulation of human Nfu activity in Fe-S cluster delivery-characterization of the interaction between Nfu and the HSPA9/Hsc20 chaperone complex.Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry.
P2860
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P2860
Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@en
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@nl
type
label
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@en
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@nl
prefLabel
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@en
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@nl
P2093
P356
P1433
P1476
Iron-sulfur cluster biosynthes ...... try and a conserved aspartate.
@en
P2093
Kristene K Surerus
Shu-Pao Wu
P304
P356
10.1021/BI0256781
P407
P577
2002-07-01T00:00:00Z