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The nitration of tyrosine residues in proteins represents a specific footprint of the formation of reactive nitrogen species (RNS) in vivo. Herein, we use fusion product of ORange Protein (ATCUN-ORP) as a vitro model system containing an ATCUN tag at N-terminus and a native tyrosine residue in the metal-cofactor binding region for the formation of 3-NO2Tyr (3-NT). The present study shows that NiII-ATCUN unusually performs nitration of tyrosine at physiological pH in presence of NO2-/SO32-/O2 system, which revealed by a characteristic absorbance band at 430 nm in basic medium and 350 nm in acidic medium (fingerprint of 3-NT). Kinetics studies showed that the formation of 3-NT depends on sulfite concentration over nitrite concentration suggested key intermediate product, oxysulfur radicals, which are detected by spin-trap (DMPO) EPR study. This study find new route in the formation of 3-NT and may link with sulfur metabolism pathway associated progression of disease states in vivo.
This article was published in the following journal.
Name: Chemistry (Weinheim an der Bergstrasse, Germany)
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An enzyme that catalyzes oxidation of sulfite to sulfate along with the reduction of FERROCYTOCHROME C to FERRICYTOCHROME C.
A MOLYBDENUM requiring enzyme that catalyzes the terminal reaction in the oxidative degradation of SULFUR AMINO ACIDS with the formation of a sulfate. A deficiency of sulfite oxidase results in sulfocysteinuria.
A NADPH-dependent oxidase that reduces hydrogen sulfite to HYDROGEN SULFIDE. It is found in many microoganisms.
A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1.
An IRON-containing protein that uses siroheme and 4Fe-4S iron-sulfur centers as prosthetic groups. It catalyzes the six-electron oxidation of AMMONIA to nitrite.
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