Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves. Igamberdiev, A. U. & Gardestrom, P. Biochimica Et Biophysica Acta-Bioenergetics, 1606(1-3):117–125, September, 2003. Place: Amsterdam Publisher: Elsevier Science Bv WOS:000185593100009doi abstract bibtex Regulation of NAD- and NADP-dependent isocitrate dehydrogenases (NAD-ICDH, EC 1.1.1.41, and NADP-ICDH, EC 1.1.1.42) by the level of reduced and oxidized pyridine nucleotides has been investigated in pea (Pisum sativum L.) leaves. The affinities of mitochondrial and cytosolic ICDH enzymes to substrates and inhibitors were determined on partially purified preparations in forward and reverse directions. From the kinetic data, it follows that NADP(+)- and NAD+-dependent isocitrate dehydrogenases in mitochondria represent a system strongly responding to the intramitochondrial NADPH and NADH levels. The NADPH, NADP(+), NADH and NAD(+) concentrations were determined by subcellular fractionation of pea leaf protoplasts using membrane filtration in mitochondria and cytosol in darkness and in the light under saturating and limiting CO2 Conditions. The cytosolic NADPH/NADP ratio was about I and almost constant both in darkness and in the light. In mitochondria, the NADPH/NADP ratio was low in darkness (0.2) and increased in the light, reaching 3 in limiting CO2 conditions compared to I in saturating CO2. At high reduction levels of NADP and NAD observed at limiting CO2 in the light, i.e. when photorespiratory glycine is the main mitochondrial substrate, isocitrate oxidation in mitochondria will be suppressed and citrate will be transported to the cytosol ('citrate valve'), where the cytosolic NADP-ICDH supplies 2-oxoglutarate for the photorespiratory ammonia refixation. (C) 2003 Elsevier B.V. All rights reserved.
@article{igamberdiev_regulation_2003,
title = {Regulation of {NAD}- and {NADP}-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves},
volume = {1606},
issn = {0005-2728},
doi = {10/frnr6s},
abstract = {Regulation of NAD- and NADP-dependent isocitrate dehydrogenases (NAD-ICDH, EC 1.1.1.41, and NADP-ICDH, EC 1.1.1.42) by the level of reduced and oxidized pyridine nucleotides has been investigated in pea (Pisum sativum L.) leaves. The affinities of mitochondrial and cytosolic ICDH enzymes to substrates and inhibitors were determined on partially purified preparations in forward and reverse directions. From the kinetic data, it follows that NADP(+)- and NAD+-dependent isocitrate dehydrogenases in mitochondria represent a system strongly responding to the intramitochondrial NADPH and NADH levels. The NADPH, NADP(+), NADH and NAD(+) concentrations were determined by subcellular fractionation of pea leaf protoplasts using membrane filtration in mitochondria and cytosol in darkness and in the light under saturating and limiting CO2 Conditions. The cytosolic NADPH/NADP ratio was about I and almost constant both in darkness and in the light. In mitochondria, the NADPH/NADP ratio was low in darkness (0.2) and increased in the light, reaching 3 in limiting CO2 conditions compared to I in saturating CO2. At high reduction levels of NADP and NAD observed at limiting CO2 in the light, i.e. when photorespiratory glycine is the main mitochondrial substrate, isocitrate oxidation in mitochondria will be suppressed and citrate will be transported to the cytosol ('citrate valve'), where the cytosolic NADP-ICDH supplies 2-oxoglutarate for the photorespiratory ammonia refixation. (C) 2003 Elsevier B.V. All rights reserved.},
language = {English},
number = {1-3},
journal = {Biochimica Et Biophysica Acta-Bioenergetics},
author = {Igamberdiev, A. U. and Gardestrom, P.},
month = sep,
year = {2003},
note = {Place: Amsterdam
Publisher: Elsevier Science Bv
WOS:000185593100009},
keywords = {NAD(P)H/NAD(P) ratio, alternative oxidase, ammonia refixation, barley leaf protoplasts, citrate valve, glycine decarboxylase, isocitrate dehydrogenase, metabolite concentrations, photorespiration, plant mitochondria, plant-mitochondria, purification, rapid fractionation, redox transfer, subcellular volumes, transhydrogenase},
pages = {117--125},
}
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From the kinetic data, it follows that NADP(+)- and NAD+-dependent isocitrate dehydrogenases in mitochondria represent a system strongly responding to the intramitochondrial NADPH and NADH levels. The NADPH, NADP(+), NADH and NAD(+) concentrations were determined by subcellular fractionation of pea leaf protoplasts using membrane filtration in mitochondria and cytosol in darkness and in the light under saturating and limiting CO2 Conditions. The cytosolic NADPH/NADP ratio was about I and almost constant both in darkness and in the light. In mitochondria, the NADPH/NADP ratio was low in darkness (0.2) and increased in the light, reaching 3 in limiting CO2 conditions compared to I in saturating CO2. At high reduction levels of NADP and NAD observed at limiting CO2 in the light, i.e. when photorespiratory glycine is the main mitochondrial substrate, isocitrate oxidation in mitochondria will be suppressed and citrate will be transported to the cytosol ('citrate valve'), where the cytosolic NADP-ICDH supplies 2-oxoglutarate for the photorespiratory ammonia refixation. (C) 2003 Elsevier B.V. All rights reserved.","language":"English","number":"1-3","journal":"Biochimica Et Biophysica Acta-Bioenergetics","author":[{"propositions":[],"lastnames":["Igamberdiev"],"firstnames":["A.","U."],"suffixes":[]},{"propositions":[],"lastnames":["Gardestrom"],"firstnames":["P."],"suffixes":[]}],"month":"September","year":"2003","note":"Place: Amsterdam Publisher: Elsevier Science Bv WOS:000185593100009","keywords":"NAD(P)H/NAD(P) ratio, alternative oxidase, ammonia refixation, barley leaf protoplasts, citrate valve, glycine decarboxylase, isocitrate dehydrogenase, metabolite concentrations, photorespiration, plant mitochondria, plant-mitochondria, purification, rapid fractionation, redox transfer, subcellular volumes, transhydrogenase","pages":"117–125","bibtex":"@article{igamberdiev_regulation_2003,\n\ttitle = {Regulation of {NAD}- and {NADP}-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves},\n\tvolume = {1606},\n\tissn = {0005-2728},\n\tdoi = {10/frnr6s},\n\tabstract = {Regulation of NAD- and NADP-dependent isocitrate dehydrogenases (NAD-ICDH, EC 1.1.1.41, and NADP-ICDH, EC 1.1.1.42) by the level of reduced and oxidized pyridine nucleotides has been investigated in pea (Pisum sativum L.) leaves. The affinities of mitochondrial and cytosolic ICDH enzymes to substrates and inhibitors were determined on partially purified preparations in forward and reverse directions. From the kinetic data, it follows that NADP(+)- and NAD+-dependent isocitrate dehydrogenases in mitochondria represent a system strongly responding to the intramitochondrial NADPH and NADH levels. The NADPH, NADP(+), NADH and NAD(+) concentrations were determined by subcellular fractionation of pea leaf protoplasts using membrane filtration in mitochondria and cytosol in darkness and in the light under saturating and limiting CO2 Conditions. The cytosolic NADPH/NADP ratio was about I and almost constant both in darkness and in the light. In mitochondria, the NADPH/NADP ratio was low in darkness (0.2) and increased in the light, reaching 3 in limiting CO2 conditions compared to I in saturating CO2. 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