Published November 26, 2003
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Journal Article
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Spectroscopy and Reactivity of a Photogenerated Tryptophan Radical in a Structurally Defined Protein Environment
Chicago
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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(NH_3)_5Cl]Cl_2 produces a tryptophan radical (W108•) with unprecedented kinetic stability. After rapid formation (k = 2.8 × 10^6 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 K_4[Mo(CN)_8] by ReAz(W108•)Zn(II) places the W108•/W108 reduction potential in the protein above 0.8 V vs NHE.
Additional Information
© 2003 American Chemical Society. Received 10 July 2003. Published online 1 November 2003. Published in print 1 November 2003. Randy Villahermosa assisted with the transient absorption measurements. J.E.M. thanks the Parsons Foundation for a graduate fellowship. Work at Cornell was supported by NSF (MCB0133546); work at Caltech was supported by NIH (DK19038).Attached Files
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Additional details
- Eprint ID
- 76695
- Resolver ID
- CaltechAUTHORS:20170419-130606164
- NSF
- MCB-0133546
- NIH
- DK19038
- Created
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2017-04-19Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field