Dramatic modulation of electron transfer in protein complexes by crosslinking.
The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein-protein interface may considerably influence the electronic coupling between redox centers.
van Amsterdam
Irene M C
IM
Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, P.O. Box 9502, 2300 RA Leiden, the Netherlands.
Ubbink
Marcellus
M
Einsle
Oliver
O
Messerschmidt
Albrecht
A
Merli
Angelo
A
Cavazzini
Davide
D
Rossi
Gian Luigi
GL
Canters
Gerard W
GW
D001400:Azurin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D003432:Cross-Linking Reagents / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D019281:Dimerization; D004579:Electron Transport; D007700:Kinetics; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics; D020836:Protein Structure, Quaternary; D011550:Pseudomonas aeruginosa / Q000737:chemistry* / Q000235:genetics; D014867:Water / Q000737:chemistry
D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D014867:Water; D001400:Azurin