Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy.
Plastocyanin and cytochrome c(6) function as electron shuttles between cytochrome f and photosystem I in the photosynthetic redox chain. To transfer electrons the partners form transient complexes, which are remarkably short-lived (milliseconds or less). Recent nuclear magnetic resonance studies have revealed details of the molecular interfaces found in such complexes. General features include a small binding site with a hydrophobic core and a polar periphery, including some charged residues. Furthermore, it was found that the interactions are relatively nonspecific. The structural information, in combination with kinetic and theoretical analyses of protein complexes, provides new insight into the nature of transient protein interactions.
Crowley
Peter B
PB
Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Ubbink
Marcellus
M
D045365:Cytochromes c6 / Q000737:chemistry; D045348:Cytochromes f / Q000737:chemistry; D004579:Electron Transport; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D010970:Plastocyanin / Q000737:chemistry*
D045365:Cytochromes c6; D045322:Photosynthetic Reaction Center Complex Proteins; D010970:Plastocyanin; D045348:Cytochromes f