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Glycolate oxidoreductase in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
Abstract Escherichia coli cells growing on glycolate as a sole source of carbon synthesise an enzyme which catalyses the oxidation of this compound to glyoxylate. The formation of glyoxylate from glycolate by extracts of such cells is dependent upon the presence of the artificial electron acceptors phenazine methosulphate and 2,6 ...
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Quinone Oxidoreductases of the Plasma Membrane

2004
Publisher Summary Quinone oxidoreductases of the plasma membrane relate functionally to the operation of a cell surface redox chain, where cytosolic NAD(P)H is oxidized. Plasma membrane quinones serve as lipid-soluble transmembrane shuttles to transfer the 2H+ + 2e- from NAD(P)H to 1/2 O2 to form water.
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Pyridine Nucleotide — Disulfide Oxidoreductases

1980
Electron transfer between pyridine nucleotides and disulfide compounds is catalyzed by three flavoproteins which are well characterized. Lipoamide dehydrogenase reoxidizes reduced lipoamide (lip-(SH)2) by NAD+. Glutathione reductase catalyzes reduction of glutathione (GSSG) by NADPH. Thioredoxin reductase catalyzes the reduction of oxidized thioredoxin
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Oxidoreductases