Interaction of ferredoxin with ferredoxin:NADP reductase: effects of chemical modification of ferredoxin |
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| Authors: | B J Vieira D J Davis |
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| Affiliation: | 1. Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102A, HR-10 000, Zagreb, Croatia;2. Department of Molecular Diagnostics, Austrian Institute of Technology GmbH, Giefinggasse 2, AU-1210, Wien, Austria;3. Department of Molecular Biology, Rudjer Bošković Institute, Bijenička cesta 54, HR-10000, Zagreb, Croatia;1. Molecular Plant Biology, Department of Biochemistry, University of Turku, FI-20014 Turku, Finland;2. Munich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, D-81377 Munich, Germany;3. Department of Biology I, Botany, Ludwig-Maximilians-Universität München, Groβhaderner Strasse 2–4, D-82152 Planegg-Martinsried, Germany;4. Department of Biology I, Plant Metabolism Group, Ludwig-Maximilians-Universität München, Groβhaderner Strasse 2–4, D-82152 Planegg-Martinsried, Germany;5. Institute for Plant Biochemistry, Cluster of Excellence on Plant Sciences (CEPLAS), Universitätsstrasse 1, D-40225 Düsseldorf, Germany |
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| Abstract: | Chemical modification studies have been conducted on spinach ferredoxin to determine the nature of the groups on ferredoxin involved in its interaction with its reaction partners. Modification of a limited number (three or four) carboxyl groups or of the single histidine residue resulted in a decreased ability of ferredoxin to participate in NADP photoreduction but not in cytochrome c photoreduction, suggesting that these groups may be involved in interaction with ferredoxin:NADP reductase but are not involved in interaction with the reducing side of Photosystem I. In contrast, modification of amino groups or the single arginine residue on ferredoxin had little effect on the ability of ferredoxin to participate in NADP photoreduction, suggesting these groups are not involved in the interaction of ferredoxin with either ferredoxin:NADP reductase or the reducing side of Photosystem I. Attempts to modify tyrosine residues on ferredoxin resulted in destruction of the iron-sulfur center of the protein. |
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