Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hepatic microsomal NADPH cytochrome c reductase from nonhuman primate (Macaca mulatta) has been purified 76 fold by the combination of anion exchange, affinity and molecular sieve chromatographies. The purified preparation had approximate molecular wt of 63 kDa and carried out NADPH oxidation, cytochrome c reduction, 2,6-dichlorophenol indophenol (DCIP) reduction and production of superoxide anions (O2-.). The enhancement in NADPH cytochrome c reductase catalyzed NADPH oxidation by metal chelators viz. ethylenediaminetetra-acetic acid (EDTA)-FeCl3 and diethylenetriaminepenta-acetic acid (DTPA)-FeCl3 was dramatically higher than the enhancement in the reduction of cytochrome c and DCIP. DTPA-FeCl3 was found to be more potent stimulator of NADPH oxidation as compared to EDTA-FeCl3, but both had similar potency as for reduction of cytochrome c and DCIP were concerned. Superoxide dismutase (SOD) decreased EDTA-FeCl3 enhanced reduction of cytochrome c by 15%, but had no effect on the NADPH oxidation and DCIP reduction, whereas it significantly enhanced DTPA-FeCl3 stimulated NADPH oxidation, decreased cytochrome c reduction by 8% and did not affect DCIP reduction. In addition, SOD almost completely blocked the NADPH cytochrome c reductase catalyzed superoxide anion production. The results demonstrate that like rodents and lagomorphs, the hepatic microsomal NADPH cytochrome c reductase in nonhuman primate, Macaca mulatta can carry out single electron reduction of molecular oxygen.
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PMID:Purification and characterization of hepatic microsomal NADPH cytochrome c reductase from rhesus monkey (Macaca mulatta). 801 90

This mini-review summarizes results of studies on the oxidation of proteins and low-density lipoprotein (LDL) by various mixed-function oxidation (MFO) systems. Oxidation of LDL by the O2/FeCl3/H2O2/ascorbate MFO system is dependent on all four components and is much greater when reactions are carried out in the presence of a physiological bicarbonate/CO2 buffer system as compared to phosphate buffer. However, FeCl3 in this system could be replaced by hemin or the heme-containing protein, hemoglobin, or cytochrome c. Oxidation of LDL by the O2/cytochrome P450 cytochrome c reductase/NADPH/FeCl3 MFO system is only slightly higher (25%) in the bicarbonate/CO2 buffer as compared to phosphate buffer, but is dependent on all components except FeCl3. Omission of FeCl3 led to a 60% loss of activity. These results suggest that peroxymonobicarbonate and/or free radical derivatives of bicarbonate ion and/or CO2 might contribute to LDL oxidation by these MFO systems.
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PMID:Protein oxidation by the cytochrome P450 mixed-function oxidation system. 1614 Feb 63