Redox characterization of the FeS protein MitoNEET and impact of thiazolidinedione drug binding.
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Allostery in the ferredoxin protein motif does not involve a conformational switchStructure and Molecular Evolution of CDGSH Iron-Sulfur DomainsAllosteric control in a metalloprotein dramatically alters function.Binding of Nitric Oxide in CDGSH-type [2Fe-2S] Clusters of the Human Mitochondrial Protein Miner2.Conserved hydrogen bonding networks of MitoNEET tune Fe-S cluster binding and structural stability.Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast.The mitochondrial complex I activity is reduced in cells with impaired cystic fibrosis transmembrane conductance regulator (CFTR) function.Interdomain communication revealed in the diabetes drug target mitoNEETFacile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor proteinNADPH inhibits [2Fe-2S] cluster protein transfer from diabetes drug target MitoNEET to an apo-acceptor protein.Protonation and concerted proton-electron transfer reactivity of a bis-benzimidazolate ligated [2Fe-2S] model for Rieske clustersCharacterization of the [2Fe-2S] cluster of Escherichia coli transcription factor IscR.Protonation and Proton-Coupled Electron Transfer at S-Ligated [4Fe-4S] ClustersNovel ligands that target the mitochondrial membrane protein mitoNEETCompetition of zinc ion for the [2Fe-2S] cluster binding site in the diabetes drug target protein mitoNEET.Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.Electron transfer and proton-coupled electron transfer reactivity and self-exchange of synthetic [2Fe-2S] complexes: models for Rieske and mitoNEET clustersModel of the MitoNEET [2Fe-2S] Cluster Shows Proton Coupled Electron Transfer.Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase.Engineering the redox potential over a wide range within a new class of FeS proteins.Molecular Dynamics Simulations of the [2Fe-2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release.Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET.The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.Distinguishing the Protonation State of the Histidine Ligand to the Oxidized Iron-Sulfur Cluster from the MitoNEET Family of Proteins.Fe-S Clusters Emerging as Targets of Therapeutic Drugs.The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.
P2860
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P2860
Redox characterization of the FeS protein MitoNEET and impact of thiazolidinedione drug binding.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Redox characterization of the ...... hiazolidinedione drug binding.
@en
Redox characterization of the ...... hiazolidinedione drug binding.
@nl
type
label
Redox characterization of the ...... hiazolidinedione drug binding.
@en
Redox characterization of the ...... hiazolidinedione drug binding.
@nl
prefLabel
Redox characterization of the ...... hiazolidinedione drug binding.
@en
Redox characterization of the ...... hiazolidinedione drug binding.
@nl
P2093
P2860
P356
P1433
P1476
Redox characterization of the ...... hiazolidinedione drug binding.
@en
P2093
Daniel W Bak
John A Zuris
Mark L Paddock
Patricia A Jennings
P2860
P304
10193-10195
P356
10.1021/BI9016445
P407
P577
2009-11-01T00:00:00Z