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Oxidation of Reduced Nicotinamide Adenine Dinucleotide Phosphate by Isolated Corn Mitochondria
Author(s) -
D. E. Koeppe,
Raymond J. Miller
Publication year - 1972
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.49.3.353
Subject(s) - nicotinamide adenine dinucleotide phosphate , chemistry , nad+ kinase , calcium , mitochondrion , nicotinamide adenine dinucleotide , phosphate , biochemistry , adenine nucleotide , redox , adenosine diphosphate , oxygen , enzyme , inorganic chemistry , nucleotide , organic chemistry , biology , oxidase test , gene , platelet , platelet aggregation , immunology
Isolated corn (Zea mays L.) mitochondria were found to oxidize reduced nicotinamide adenine dinucleotide phosphate in a KCl reaction medium. This oxidation was dependent on the presence of calcium or phosphate or both. Strontium and manganese substituted for calcium, but magnesium or barium did not. The oxidation of NADPH produced contraction of mitochondria swollen in KCl. Further evidence that the oxidation of NADPH was coupled was observed in respiratory control and adenosine diphosphate-oxygen ratios that were comparable to those reported for reduced nicotinamide adenine dinucleotide. The pathways of electron flow from NADH and NADPH were compared through the addition of electron transport inhibitors. The only difference between the two dinucleotides was that amytal was found to inhibit almost totally the state 3 oxidation of NADPH, but had little effect on the state 3 oxidation of NADH. The hypothetical pathways for electron flow from NADPH are discussed, as are the possible sites of calcium and phosphate stimulation.

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