1R1C

PSEUDOMONAS AERUGINOSA W48F/Y72F/H83Q/Y108W-AZURIN RE(PHEN)(CO)3(HIS107)

Summary for 1R1C

• Entry DOI: 10.2210/pdb1r1c/pdb
• Descriptor: Azurin, COPPER (I) ION, (1,10 PHENANTHROLINE)-(TRI-CARBON MONOXIDE) RHENIUM (I), ... (4 entities in total)
• Functional Keywords: blue-copper, electron-transfer, rhenium, tunneling, radical, epr, electron transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 4
• Total formula weight: 57775.15

Authors

Miller, J.E.,Gradinaru, C.,Crane, B.R.,Di Bilio, A.J. (deposition date: 2003-09-23, release date: 2003-09-30, Last modification date: 2024-12-25)

Primary citation

Miller, J.E.,Gradinaru, C.,Crane, B.R.,Di Bilio, A.J.,Wehbi, W.A.,Un, S.,Winkler, J.R.,Gray, H.B.
Spectroscopy and reactivity of a photogenerated tryptophan radical in a structurally defined protein environment
J.Am.Chem.Soc., 125:14220-14221, 2003

PubMed Abstract: Near-UV irradiation of structurally characterized [Re(I)(CO)3(1,10-phenanthroline)(Q107H)](W48F/Y72F/H83Q/Y108W)AzM(II) [Az = Pseudomonas aeruginosa azurin, M = Cu, Zn]/[Co(NH3)5Cl]Cl2 produces a tryptophan radical (W108*) with unprecedented kinetic stability. After rapid formation (k = 2.8 x 106 s-1), the radical persists for more than 5 h at room temperature in the folded ReAzM(II) structure. The absorption spectrum of ReAz(W108*)M(II) exhibits maxima at 512 and 536 nm. Oxidation of K4[Mo(CN)8] by ReAz(W108*)Zn(II) places the W108*/W108 reduction potential in the protein above 0.8 V vs NHE.

PubMed: 14624538
DOI: 10.1021/ja037203i

Experimental method

X-RAY DIFFRACTION (1.9 Å)