Protein tuning of excited-state charge-transfer dynamics in azurin

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.