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Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p.
Reduced Ero1p can catalyze reduction of exogenous FAD in solution and drive disulfide bond formation under anaerobic conditions in the endoplasmic reticulum. Expand
Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes.
It is suggested that QSOX enzymes play a significant role in oxidative folding of a large variety of proteins in a wide range of multicellular organisms. Expand
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity.
Data suggest that this poorly understood flavoenzyme may not function as a sulfhydryl oxidase within the mitochondrial intermembrane space but may communicate with the respiratory chain via the mediation of cytochrome c. Expand
Quantification of thiols and disulfides.
The toolbox available to the experimentalist for the chemical determination of thiols and disulfides is surveyed, with a focus on the key chemical aspects of current methodology, together with identifying potential difficulties inherent in their experimental implementation. Expand
Acyl-CoA dehydrogenases. A mechanistic overview.
This work discusses the main factors that bring about catalysis, promote specificity and determine the selective transfer of electrons to electron transferring flavoprotein in medium chain acyl-CoA dehydrogenase. Expand
An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion.
The convenience of the ferricenium method suggests it may be generally useful as a screening assay for a number of acyl-CoA dehydrogenases, and avoids the necessity of purifying substantial amounts of electron transferring flavoprotein. Expand
New water-soluble phosphines as reductants of peptide and protein disulfide bonds: reactivity and membrane permeability.
Molecular modeling suggests that the nucleophilic phosphorus of TCEP is more sterically crowded than the thiolate of DTT, contributing to the lower reactivity of the phosphine with protein disulfides at this pH. Expand
Sulfhydryl Oxidase from Egg White
Data show that sulfhydryl oxidase and protein disulfide isomerase can cooperate in vitro in the generation and rearrangement of native disulfides pairings and a possible role for the oxidase in the protein secretory pathway in vivo is discussed. Expand
Homology between Egg White Sulfhydryl Oxidase and Quiescin Q6 Defines a New Class of Flavin-linked Sulfhydryl Oxidases*
The flavin-dependent sulfhydryl oxidase from chicken egg white catalyzes the oxidation of sulfhydryl groups to disulfides with the reduction of oxygen to hydrogen peroxide. Reduced proteins are theExpand
Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.
The review compares the substrate specificity and catalytic efficiency of the QSOX enzymes with members of the Ero1 family of flavin-dependent sulfhydryl oxidases: enzymes believed to play key roles in disulfide generation in yeast and higher eukaryotes. Expand