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Reexamination of reduced pteridine cofactors behaviour by proton nuclear magnetic resonance spectroscopy and mass spectrometry
Author(s) -
Hénichart JeanPierre,
Bernier JeanLuc,
Dhondt JeanLouis,
Dautrevaux Michel,
Biserte Gérard
Publication year - 1979
Publication title -
journal of heterocyclic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.321
H-Index - 59
eISSN - 1943-5193
pISSN - 0022-152X
DOI - 10.1002/jhet.5570160740
Subject(s) - chemistry , autoxidation , mass spectrometry , hydrogen peroxide , cofactor , nuclear magnetic resonance spectroscopy , pteridine , horseradish peroxidase , aqueous solution , spectroscopy , photochemistry , organic chemistry , enzyme , chromatography , physics , quantum mechanics
In aqueous solutions, the autoxidation by air of 2‐amino‐4‐hydroxy‐6,7‐dimethyl‐5,6,7,8‐tetra‐hydropteridine, a hydroxylase cofactor, leads to the corresponding 7,8‐dihydro derivate. Oxidation by hydrogen peroxide and Horseradish peroxidase does not give a stable quinonoid form as previously claimed but affords two metabolic products. Kinetics of the two pathways and structures of the different final compounds were determined by 1 H nmr and mass spectrometry.