Complexes of Photosynthetic Redox Proteins Studied by NMR |
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| Authors: | Ubbink Marcellus |
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| Affiliation: | Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300, RA Leiden, The Netherlands, m.ubbink@chem.leidenuniv.nl. |
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| Abstract: | In the photosynthetic redox chain, small electron transfer proteins shuttle electrons between the large membrane-associated redox complexes. Short-lived but specific protein:protein complexes are formed to enable fast electron transfer. Recent nuclear magnetic resonance (NMR) studies have elucidated the binding sites on plastocyanin, cytochrome c (6) and ferredoxin. Also the orientation of plastocyanin in complex with cytochrome f has been determined. Based on these results, general features that enable the formation of such transient complexes are discussed. |
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| Keywords: | cytochrome c cytochrome c6 cytochrome f electron transfer ferredoxin FNR NMR photosynthesis plastocyanin redox protein |
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