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10.1074/jbc.M116.718734 http://scihub22266oqcxt.onion/10.1074/jbc.M116.718734 C4825006!4825006 !26867575     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26867575 &cmd=llinks): Failed to open stream: HTTP request failed! 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Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine ?-Synthase |pdf=|usr=}}{{26867575 }} gab.com Text Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine -Synthase JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26867575 #FOAvip Cystathionine ?-synthase (CBS) is a pyridoxal phosphate-dependent enzyme that catalyzes the condensation of homocysteine with serine or with cysteine to form cystathionine and either water or hydrogen sulfide, respectively. Human CBS possesses a noncatalytic heme cofactor with cysteine and histidine as ligands, which in its oxidized state is relatively unreactive. Ferric CBS (Fe(III)-CBS) can be reduced by strong chemical and biochemical reductants to Fe(II)-CBS, which can bind carbon monoxide (CO) or nitric oxide (NO(?)), leading to inactive enzyme. Alternatively, Fe(II)-CBS can be reoxidized by O2to Fe(III)-CBS, forming superoxide radical anion (O2 (??)). In this study, we describe the kinetics of nitrite (NO2 (-)) reduction by Fe(II)-CBS to form Fe(II)NO(?)-CBS. The second order rate constant for the reaction of Fe(II)-CBS with nitrite was obtained at low dithionite concentrations. Reoxidation of Fe(II)NO(?)-CBS by O2showed complex kinetic behavior and led to peroxynitrite (ONOO(-)) formation, which was detected using the fluorescent probe, coumarin boronic acid. Thus, in addition to being a potential source of superoxide radical, CBS constitutes a previously unrecognized source of NO(?)and peroxynitrite. Twit Text FOAVip Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine -Synthase ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26867575 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26867575 #FOAvip English Wikipedia <ref>{{Cite pmid|26867575 }}</ref> Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine ?-Synthase #MMPMID26867575 Carballal S ; Cuevasanta E ; Yadav PK ; Gherasim C ; Ballou DP ; Alvarez B ; Banerjee R J Biol Chem 2016[Apr]; 291 (15 ): 8004-13 PMID26867575 show ga Cystathionine ?-synthase (CBS) is a pyridoxal phosphate-dependent enzyme that catalyzes the condensation of homocysteine with serine or with cysteine to form cystathionine and either water or hydrogen sulfide, respectively. Human CBS possesses a noncatalytic heme cofactor with cysteine and histidine as ligands, which in its oxidized state is relatively unreactive. Ferric CBS (Fe(III)-CBS) can be reduced by strong chemical and biochemical reductants to Fe(II)-CBS, which can bind carbon monoxide (CO) or nitric oxide (NO(?)), leading to inactive enzyme. Alternatively, Fe(II)-CBS can be reoxidized by O2to Fe(III)-CBS, forming superoxide radical anion (O2 (??)). In this study, we describe the kinetics of nitrite (NO2 (-)) reduction by Fe(II)-CBS to form Fe(II)NO(?)-CBS. The second order rate constant for the reaction of Fe(II)-CBS with nitrite was obtained at low dithionite concentrations. Reoxidation of Fe(II)NO(?)-CBS by O2showed complex kinetic behavior and led to peroxynitrite (ONOO(-)) formation, which was detected using the fluorescent probe, coumarin boronic acid. Thus, in addition to being a potential source of superoxide radical, CBS constitutes a previously unrecognized source of NO(?)and peroxynitrite. |Carbon Monoxide/metabolism [MESH] |Cystathionine beta-Synthase/chemistry/*metabolism [MESH] |Heme/chemistry/*metabolism [MESH] |Humans [MESH] |Kinetics [MESH] |Nitric Oxide/metabolism [MESH] |Nitrites/*metabolism [MESH] |Oxidation-Reduction [MESH] |Oxygen/metabolism [MESH] |Peroxynitrous Acid/*metabolism [MESH]Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous H(epmc).pdf DeepDyve Pubget Overpricing