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
Energy flow in biological structures often requires submillisecond charge transport over long molecular distances. Kinetics modeling suggests that charge-transfer rates can be greatly enhanced by multistep electron tunneling in which redox-active amino acid side chains act as intermediate donors or acceptors. We report transient optical and infrared spectroscopic experiments that quantify the extent to which an intervening tryptophan residue can facilitate electron transfer between distant metal redox centers in a mutant Pseudomonas aeruginosa azurin. Cu(I) oxidation by a photoexcited Re(I)-diimine at position 124 on a histidine(124)-glycine(123)-tryptophan(122)-methionine(121) beta strand occurs in a few nanoseconds, fully two orders of magnitude faster than documented for single-step electron tunneling at a 19 angstrom donor-acceptor distance.
Tryptophan-accelerated electron flow through proteins.,Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB Science. 2008 Jun 27;320(5884):1760-2. PMID:18583608[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Tryptophan-accelerated electron flow through proteins. Science. 2008 Jun 27;320(5884):1760-2. PMID:18583608 doi:320/5884/1760
