z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom