Structural highlights
Function
[AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Dramatic modulation of electron transfer in protein complexes by crosslinking.,van Amsterdam IM, Ubbink M, Einsle O, Messerschmidt A, Merli A, Cavazzini D, Rossi GL, Canters GW Nat Struct Biol. 2002 Jan;9(1):48-52. PMID:11740504[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Amsterdam IM, Ubbink M, Einsle O, Messerschmidt A, Merli A, Cavazzini D, Rossi GL, Canters GW. Dramatic modulation of electron transfer in protein complexes by crosslinking. Nat Struct Biol. 2002 Jan;9(1):48-52. PMID:11740504 doi:10.1038/nsb736
