Complexes of photosynthetic redox proteins studied by NMR

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...

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Bibliographic Details
Published in:Photosynthesis research 2004-01, Vol.81 (3), p.277-287
Main Author: Ubbink, Marcellus
Format: Article
Language:English
Subjects:
Binding sites
NMR
Nuclear magnetic resonance
Proteins
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Summary: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.
ISSN:0166-8595
1573-5079
DOI:10.1023/B:PRES.0000036880.67124.e7