title: Protein denitration/modification by Escherichia coli nitrate reductase and mammalian cytochrome P-450 reductase.
abstract: The incubation of peroxynitrite (PN)-pretreated histone III-S (NH) with Escherichia coli nitrate reductase (cytochrome, NADPH/GSH-independent) and that of NADPH-treated NH (NHNADPH) with liver cytochrome P-450 reductase (NADPH-dependent) resulted in decreased 3-nitrotyrosine immunoreactivity found in Western blot analysis. Additionally, increased nitrate was noted as an end product of these reactions. These findings imply that varied enzymatic denitration/modification of NO/PN-reacted protein, either with or without a reductant, may be important in regulating related signal transduction cascade(s) and relieving oxidative stress.
authors.affiliation: Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114, USA. kuow@cookman.edu
authors.forename: Wu-Nan
authors.initials: WN
authors.lastname: Kuo
authors.forename: Joseph M
authors.initials: JM
authors.lastname: Kocis
authors.forename: Jenny Kreahling
authors.initials: JK
authors.lastname: Webb
mesh_terms: D000818:Animals; D004926:Escherichia coli / Q000201:enzymology*; D006657:Histones / Q000378:metabolism; D008956:Models, Chemical; D009249:NADP / Q000737:chemistry; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D050901:Nitrate Reductase; D009565:Nitrate Reductases / Q000378:metabolism*; D009566:Nitrates / Q000378:metabolism*; D030421:Peroxynitrous Acid / Q000737:chemistry; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000032:analysis
chemical_list: D006657:Histones; D009566:Nitrates; D030421:Peroxynitrous Acid; C002744:3-nitrotyrosine; D014443:Tyrosine; D009249:NADP; D009251:NADPH-Ferrihemoprotein Reductase; D009565:Nitrate Reductases; D050901:Nitrate Reductase