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Updated: Oct 2, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Protein denitration/modification by Escherichia coli nitrate reductase and mammalian cytochrome P-450 reductase
Wu-Nan Kuo1, Joseph M Kocis, Jenny Kreahling Webb
1Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114, USA. kuow@cookman.edu
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.
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