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1r1c

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(New page: 200px<br /><applet load="1r1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1c, resolution 1.90&Aring;" /> '''PSEUDOMONAS AERUGINO...)
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Revision as of 23:04, 20 November 2007


1r1c, resolution 1.90Å

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

Overview

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 × 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.

About this Structure

1R1C is a Single protein structure of sequence from Pseudomonas aeruginosa with CU1 and REP as ligands. Full crystallographic information is available from OCA.

Reference

Spectroscopy and reactivity of a photogenerated tryptophan radical in a structurally defined protein environment., Miller JE, Gradinaru C, Crane BR, Di Bilio AJ, Wehbi WA, Un S, Winkler JR, Gray HB, J Am Chem Soc. 2003 Nov 26;125(47):14220-1. PMID:14624538

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