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10.1074/jbc.M117.775981 http://scihub22266oqcxt.onion/10.1074/jbc.M117.775981 C5519355!5519355 !28533431     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28533431 &cmd=llinks): Failed to open stream: HTTP request failed! 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Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site |pdf=|usr=}}{{28533431 }} gab.com Text Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28533431 #FOAvip Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1. Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site. Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment. Twit Text FOAVip Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28533431 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28533431 #FOAvip English Wikipedia <ref>{{Cite pmid|28533431 }}</ref> Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site #MMPMID28533431 Fetherolf MM ; Boyd SD ; Taylor AB ; Kim HJ ; Wohlschlegel JA ; Blackburn NJ ; Hart PJ ; Winge DR ; Winkler DD J Biol Chem 2017[Jul]; 292 (29 ): 12025-12040 PMID28533431 show ga Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1. Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site. Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment. |*Models, Molecular [MESH] |*Protein Processing, Post-Translational [MESH] |Amino Acid Substitution [MESH] |Apoenzymes/chemistry/genetics/metabolism [MESH] |Binding Sites [MESH] |Copper/*metabolism [MESH] |Crystallography, X-Ray [MESH] |Cysteine/metabolism [MESH] |Cystine/*metabolism [MESH] |Enzyme Activation [MESH] |Enzyme Stability [MESH] |Humans [MESH] |Ligands [MESH] |Molecular Chaperones/chemistry/genetics/*metabolism [MESH] |Mutagenesis, Site-Directed [MESH] |Mutation [MESH] |Oxidation-Reduction [MESH] |Protein Conformation [MESH] |Protein Interaction Domains and Motifs [MESH] |Recombinant Proteins/chemistry/metabolism [MESH] |Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism [MESH]Copper-zinc superoxide dismutase is activated through a sulfenic acid (epmc).pdf DeepDyve Pubget Overpricing