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