The Respiratory Chain of Plant Mitochondria VI. Flavoprotein Components of the Respiratory Chain of Mung Bean Mitochondria

The Respiratory Chain of Plant Mitochondria VI. Flavoprotein Components of the Respiratory Chain... Bayard T. Storey 1 Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104 Abstract Redox changes of the flavoproteins of mung bean ( Phaseolus aureus ) mitochondria were measured by differential absorbance at 468 to 493 nanometers and by fluorescence emission above 500 nanometers excited at 436 nanometers. Four flavoproteins are distinguishable by the ratio of their fluorescence to absorbance changes, and by their requirement, or lack of it, for energy-linked reverse electron transport for reduction by succinate. Two flavoproteins are reduced by succinate in fully depleted mitochondria which lack the capacity for reverse electron transport. These are designated Fp ha and Fp hf and have fluorescence to absorbance ratios of 0 and 1.4, respectively. The two flavoproteins have the same half-time for oxidation, but Fp hf is reduced more slowly than Fp ha by substrate in the presence of cyanide. One flavoprotein with a fluorescence to absorbance ratio of 0 is not reduced by succinate in anaerobic, fully depleted mitochondria, but is rapidly reduced on subsequent addition of malate; it is designated Fp m . The fourth distinguishable flavoprotein component is reducible by succinate in an energy-linked reaction, even in partially depleted mitochondria. This component has a fluorescence to absorbance ratio of 3.8 and is designated Fp 1f . In addition to these four flavoproteins reducible by substrates, there is a highly fluorescent flavin-containing component in or associated with these mitochondria, which is rapidly reduced by dithionite. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png

The Respiratory Chain of Plant Mitochondria VI. Flavoprotein Components of the Respiratory Chain of Mung Bean Mitochondria

Jul 1, 1970

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Publisher
American Society of Plant Biologist
Copyright
Copyright © 1970 by the American Society of Plant Biologists
ISSN
1532-2548
eISSN
0032-0889
DOI
10.1104/pp.46.1.13
Publisher site
See Article on Publisher Site

Abstract

Bayard T. Storey 1 Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104 Abstract Redox changes of the flavoproteins of mung bean ( Phaseolus aureus ) mitochondria were measured by differential absorbance at 468 to 493 nanometers and by fluorescence emission above 500 nanometers excited at 436 nanometers. Four flavoproteins are distinguishable by the ratio of their fluorescence to absorbance changes, and by their requirement, or lack of it, for energy-linked reverse electron transport for reduction by succinate. Two flavoproteins are reduced by succinate in fully depleted mitochondria which lack the capacity for reverse electron transport. These are designated Fp ha and Fp hf and have fluorescence to absorbance ratios of 0 and 1.4, respectively. The two flavoproteins have the same half-time for oxidation, but Fp hf is reduced more slowly than Fp ha by substrate in the presence of cyanide. One flavoprotein with a fluorescence to absorbance ratio of 0 is not reduced by succinate in anaerobic, fully depleted mitochondria, but is rapidly reduced on subsequent addition of malate; it is designated Fp m . The fourth distinguishable flavoprotein component is reducible by succinate in an energy-linked reaction, even in partially depleted mitochondria. This component has a fluorescence to absorbance ratio of 3.8 and is designated Fp 1f . In addition to these four flavoproteins reducible by substrates, there is a highly fluorescent flavin-containing component in or associated with these mitochondria, which is rapidly reduced by dithionite.

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