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FAD binding

Known as: oxidized flavin adenine dinucleotide binding, oxidized flavine-adenine dinucleotide binding 
Interacting selectively and non-covalently with the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of… 
National Institutes of Health

Papers overview

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2006
2006
Mutations in the FAD Binding Domain Cause Stress-induced Misoxidation of the Endoplasmic Reticulum Oxidoreductase Ero1β*
Disulfide bond catalysis is an essential component of protein biogenesis in the secretory pathway, from yeast through to man. In… 
2001
2001
Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase.
Each flavoprotein subunit (alpha or PchF) of the alpha(2)beta(2) flavocytochrome p-cresol methylhydroxylase (PCMH) from… 
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