日本植物生理学会年会およびシンポジウム 講演要旨集
Supplement to Plant and Cell Physiology Vol. 45
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Subplastidal localization and Fd-interaction of maize leaf Fd-NADP+ reductase isoenzymes as studied by Fd-affinity chromatography
*奥谷 聡志ハンケ ガイ長谷 俊治
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p. 504

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In chloroplasts, Fd forms an electron transfer complex with redox enzymes, such as Fd:NADP+ oxidoreductase(FNR), sulfite reductase, nitrite reductase and glutamate synthase. Fd therefore influences redox metabolism through the formation of intermolecular electron transfer complexes, and these are the subject of our research.
Two maize leaf FNR isozymes;L-FNR1 and L-FNR2, have previously been described and we have also identified a new L-FNR. Chloroplast fractionation revealed L-FNR1 was located at the thylakoid membrane, new L-FNR in the stroma and L-FNR2 in both fractions. Using Fd-affinity chromatography with wild type and mutant Fd-resin columns we found interaction of different FNR isoenzymes strongly depend on specific Fd amino acid residues. Therefore, despite very high sequence homology, these L-FNR isoenzymes vary dramatically in location and Fd interaction.
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© 2004 by The Japanese Society of Plant Physiologists
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