Disulfide bond formation, a race between FAD and oxygen.
The long-running race to find the source of oxidizing potential for disulfide bond formation is over. The winner is one of the first contestants to enter: oxygen.
Bardwell
James C A
JC
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor 48109, USA.
D000818:Animals; D004220:Disulfides / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D008562:Membrane Glycoproteins; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D010100:Oxygen / Q000378:metabolism*; D011387:Prokaryotic Cells / Q000378:metabolism*; D017510:Protein Folding
D004220:Disulfides; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D005182:Flavin-Adenine Dinucleotide; C405327:ERO1A protein, human; C491864:Ero1l protein, mouse; D010088:Oxidoreductases; D010100:Oxygen