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Complexes of photosynthetic redox proteins studied by NMR

Journal

PHOTOSYNTHESIS RESEARCH
Volume 81, Issue 3, Pages 277-287

Publisher

KLUWER ACADEMIC PUBL
DOI: 10.1023/B:PRES.0000036880.67124.e7

Keywords

cytochrome c; cytochrome c(6); cytochrome f; electron transfer; ferredoxin; FNR; NMR; photosynthesis; plastocyanin; redox protein

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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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