Publication | Closed Access
Covalently Bound Flavin in <scp>d</scp>‐6‐Hydroxynicotine Oxidase from <i>Arthrobacter oxidans</i>
26
Citations
5
References
1973
Year
Redox SignalingD ‐6‐Hydroxynicotine OxidaseOxysterolBiochemistryNatural SciencesBound FlavinFlavin NucleusMolecular BiologyArthrobacter OxidansPeptide ScienceReactive Oxygen SpecieChemical BiologyMedicineRedox BiologyOxidative Stress
d ‐6‐Hydroxynicotine oxidase from Arthrobacter oxidans was previously shown to contain FAD covalently bound to the N‐3 of a histidyl residue of the apoprotein via the 8α‐methylene group of the flavin nucleus. For elucidating the structure around the flavin centre a tryptic‐chymotryptic FAD‐peptide from d ‐6‐hydroxynicotine oxidase was isolated and purified. The amino acid sequence of this FAD‐peptide was found to be Ser‐Gly‐Gly‐Asn‐Asn‐Pro‐Asp‐His‐Tyr‐(Gln‐Pro)‐Ala.
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