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10.1089/ars.2013.5397 http://scihub22266oqcxt.onion/10.1089/ars.2013.5397 C4523048!4523048 !25314640     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25314640 &cmd=llinks): Failed to open stream: HTTP request failed! 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Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide |pdf=|usr=}}{{25314640 }} gab.com Text Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide JO: Antioxid Redox Signal http://www.kidney.de/pget.php?&tw=1&pmid=25314640 #FOAvip AIMS: Recent studies suggest that the molybdenum enzymes xanthine oxidase, aldehyde oxidase, and mARC exhibit nitrite reductase activity at low oxygen pressures. However, inhibition studies of xanthine oxidase in humans have failed to block nitrite-dependent changes in blood flow, leading to continued exploration for other candidate nitrite reductases. Another physiologically important molybdenum enzyme?sulfite oxidase (SO)?has not been extensively studied. RESULTS: Using gas-phase nitric oxide (NO) detection and physiological concentrations of nitrite, SO functions as nitrite reductase in the presence of a one-electron donor, exhibiting redox coupling of substrate oxidation and nitrite reduction to form NO. With sulfite, the physiological substrate, SO only facilitates one turnover of nitrite reduction. Studies with recombinant heme and molybdenum domains of SO indicate that nitrite reduction occurs at the molybdenum center via coupled oxidation of Mo(IV) to Mo(V). Reaction rates of nitrite to NO decreased in the presence of a functional heme domain, mediated by steric and redox effects of this domain. Using knockdown of all molybdopterin enzymes and SO in fibroblasts isolated from patients with genetic deficiencies of molybdenum cofactor and SO, respectively, SO was found to significantly contribute to hypoxic nitrite signaling as demonstrated by activation of the canonical NO-sGC-cGMP pathway. INNOVATION: Nitrite binds to and is reduced at the molybdenum site of mammalian SO, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts. CONCLUSION: SO is a putative mammalian nitrite reductase, catalyzing nitrite reduction at the Mo(IV) center. Twit Text FOAVip Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide ????Antioxid Redox Signal http://www.kidney.de/pget.php?&tw=1&pmid=25314640 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25314640 #FOAvip English Wikipedia <ref>{{Cite pmid|25314640 }}</ref> Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide #MMPMID25314640 Wang J ; Krizowski S ; Fischer-Schrader K ; Niks D ; Tejero J ; Sparacino-Watkins C ; Wang L ; Ragireddy V ; Frizzell S ; Kelley EE ; Zhang Y ; Basu P ; Hille R ; Schwarz G ; Gladwin MT Antioxid Redox Signal 2015[Aug]; 23 (4 ): 283-94 PMID25314640 show ga AIMS: Recent studies suggest that the molybdenum enzymes xanthine oxidase, aldehyde oxidase, and mARC exhibit nitrite reductase activity at low oxygen pressures. However, inhibition studies of xanthine oxidase in humans have failed to block nitrite-dependent changes in blood flow, leading to continued exploration for other candidate nitrite reductases. Another physiologically important molybdenum enzyme?sulfite oxidase (SO)?has not been extensively studied. RESULTS: Using gas-phase nitric oxide (NO) detection and physiological concentrations of nitrite, SO functions as nitrite reductase in the presence of a one-electron donor, exhibiting redox coupling of substrate oxidation and nitrite reduction to form NO. With sulfite, the physiological substrate, SO only facilitates one turnover of nitrite reduction. Studies with recombinant heme and molybdenum domains of SO indicate that nitrite reduction occurs at the molybdenum center via coupled oxidation of Mo(IV) to Mo(V). Reaction rates of nitrite to NO decreased in the presence of a functional heme domain, mediated by steric and redox effects of this domain. Using knockdown of all molybdopterin enzymes and SO in fibroblasts isolated from patients with genetic deficiencies of molybdenum cofactor and SO, respectively, SO was found to significantly contribute to hypoxic nitrite signaling as demonstrated by activation of the canonical NO-sGC-cGMP pathway. INNOVATION: Nitrite binds to and is reduced at the molybdenum site of mammalian SO, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts. CONCLUSION: SO is a putative mammalian nitrite reductase, catalyzing nitrite reduction at the Mo(IV) center. |Coenzymes/*chemistry [MESH] |Electron Transport [MESH] |Fibroblasts/enzymology/metabolism [MESH] |Heme/chemistry [MESH] |Humans [MESH] |Metalloproteins/*chemistry [MESH] |Molybdenum Cofactors [MESH] |Molybdenum/chemistry [MESH] |Nitric Oxide/*chemistry/metabolism [MESH] |Nitrites/*chemistry/metabolism [MESH] |Oxidation-Reduction [MESH] |Protein Structure, Tertiary [MESH] |Pteridines/*chemistry [MESH] |Signal Transduction [MESH]Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domai(epmc).pdf DeepDyve Pubget Overpricing