Azurins Raman spectra

Fig. 15. Resonance Raman spectra of three blue copper proteins A. denitrificans azurin at 90 K (568.2 nm excitation), P. aeruginosa azurin at 12 K (647.1 nm excitation), and Populus nigra plastocyanin at 12 K (604 nm excitation).

Azurins, 651,652 electron transfer reactions, 653 NMR, 652 Raman spectra, 652 spectra, 652 Azurite structure, 849 

Figure 28 RR spectra (77 K) of Ni(II)-substituted P. aeruginosa azurin obtained with indicated excitation wavelengths. Asterisks indicate ice Raman bands

Figure 29 Low-temperature (77 K) RR spectra of P. aeruginosa azurin obtained in the(A) 100-500cm" and (B) 500-1000cm" regions on (a) native Cu(ll) protein (647.1-nm excitation) and (b) its Ni(ll)-substituted derivative (413.1-nm excitation). Asterisks indicate ice Raman bands

Azoresorcinol, pyridyl-metal complexes dyes, 6, 74 Azurins, 6, 651, 652 copper(II) complexes, 2, 772 5, 721 electron transfer reactions, 6, 653 NMR, 6, 652 Raman spectra, 6, 652 spectra, 6, 652 thioether complexes, 2, 557 Azurite 

Coherent Raman detected EPR spectroscopy is a new experimental method which combines optical and EPR transitions. It was applied for the first time to a bioinolecule, azurin. The information obtained allows to test electronic and structural models of the Cu site to be probed.23 In a subsequent report the same group of authors has applied microwave modulated circular dichroism to unravel individual resonance lines in overlapping spectra and to assign them to specific electronic transitions.24 

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