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Protein tuning of excited-state charge-transfer dynamics in azurin
- Source :
- Journal of Physical Chemistry B. Oct 29, 1998, Vol. 102 Issue 44, p8923, 7 p.
- Publication Year :
- 1998
-
Abstract
- The excited-state charge-transfer dynamics of azurin from Alcaligenes denitrificans (AD) has been measured with resonance Raman spectroscopy. The obtained data are then compared with values for Pseudomonas aeruginosa (PA). Azurin is a 14.6 kDa blue copper protein found in denitrifying bacteria which transports electrons from aromatic amine dehydrogenase to cytochrome c and/or nitrite reductase. Results show that azurin from AD has an inner-sphere reorganizatin energy of 0.26 eV. Differences in azurin for PA and AD are due to the chromophore structure and protein environment at the copper site.
Details
- ISSN :
- 15206106
- Volume :
- 102
- Issue :
- 44
- Database :
- Gale General OneFile
- Journal :
- Journal of Physical Chemistry B
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.53941946