The interaction of reduced nicotinamide–adenine dinucleotide phosphate with reduced nicotinamide–adenine dinucleotide–ubiquinone reductase from bovine heart mitochondria
- 15 July 1976
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 158 (1) , 149-151
- https://doi.org/10.1042/bj1580149
Abstract
Reduction of the chromophores of mitochondrial NADH-ubiquinone reductase by NADPH reaches only 50% of the extent of reduction by NADH, monitored at 450 nm. This effect is due to autoxidation of an enzyme component at a higher rate than its reduction by NADPH.This publication has 8 references indexed in Scilit:
- The effects of proteolytic digestion by trypsin on the structure and catalytic properties of reduced nicotinamide-adenine dinucleotide dehydrogenase from bovine heart mitochondriaBiochemical Journal, 1976
- Oxidation of NADPH by submitochondrial particles from beef heart in complete absence of transhydrogenase activity from NADPH to NAD.Journal of Biological Chemistry, 1975
- Pyridine nucleotide transhydrogenase activity of soluble cardiac NADH dehydrogenase and particulate NADH-ubiquinone reductaseBiochemical and Biophysical Research Communications, 1974
- Interactions of reduced and oxidized triphosphopyridine nucleotides with the electron-transport system of bovine heart mitochondriaBiochemistry, 1973
- On the oxidation of reduced nicotinamide dinucleotide phosphate by submitochondrial particles from beef heartBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- Spectrophotometric observations on the oxidation-reduction cycle of the respiratory chain-linked reduced nicotinamide-adenine dinucleotide dehydrogenaseBiochemistry, 1970
- STUDIES ON ELECTRON TRANSFER SYSTEM .40. PREPARATION AND PROPERTIES OF MITOCHONDRIAL DPNH-COENZYME Q REDUCTASE1962
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951