2I7O

Structure of Re(4,7-dimethyl-phen)(Thr124His)(Lys122Trp)(His83Gln)AzCu(II), a Rhenium modified Azurin mutant

Summary for 2I7O

• Entry DOI: 10.2210/pdb2i7o/pdb
• Related: 1BEX
• Descriptor: Azurin, COPPER (II) ION, (1,10 PHENANTHROLINE)-(TRI-CARBON MONOXIDE) RHENIUM (I), ... (4 entities in total)
• Functional Keywords: azurin, rhenium, elecron transfer, tryptophan, electron transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 1
• Total formula weight: 14586.91

Authors

Sudhamsu, J.,Crane, B.R. (deposition date: 2006-08-31, release date: 2007-08-14, Last modification date: 2024-11-06)

Primary citation

Shih, C.,Museth, A.K.,Abrahamsson, M.,Blanco-Rodriguez, A.M.,Di Bilio, A.J.,Sudhamsu, J.,Crane, B.R.,Ronayne, K.L.,Towrie, M.,Vlcek, A.,Richards, J.H.,Winkler, J.R.,Gray, H.B.
Tryptophan-accelerated electron flow through proteins.
Science, 320:1760-1762, 2008

PubMed Abstract: 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.

PubMed: 18583608
DOI: 10.1126/science.1158241

Experimental method

X-RAY DIFFRACTION (1.5 Å)