Abstract
A detailed picture of the unique electronic structure of active sites in copper proteins is essential to our understanding of their biological functions. This has been achieved through a combination of complementary spectroscopic techniques, chemical perturbations, and parallel studies on copper complexes which serve as spectral analogues. These studies provide a basis for the generation of a “spectroscopically effective” picture of the active site and allow a correlation of changes in geometric and electronic structure with variation in function. When combined with high-resolution crystallographic information, single crystal spectral studies allow a correlation of electronic features with specific geometric features and provide a great deal of insight into the bonding at the site.
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Abbreviations
- CD:
-
Circular dichroism
- cm−1 :
-
Wavenumber
- CT:
-
Charge transfer
- Cys:
-
Cysteine
- ENDOR:
-
Electron nuclear double resonance
- EPR:
-
Electron paramagnetic resonance
- ESCA:
-
Electron spectroscopy for chemical analysis
- eV:
-
Electron volt
- EXAFS:
-
Extended x-ray absorption fine structure
- GHz:
-
Gigahertz
- His:
-
Histidine
- IR:
-
Infrared
- IT:
-
Intervalent transfer
- LEFE:
-
Linear electric field effect
- MCD:
-
Magnetic circular dichroism
- Met:
-
Methionine
- NMR:
-
Nuclear magnetic resonance
- SCF-Xα-SW:
-
Self-consistent field Xα scattered wave
- SOD:
-
Superoxide dismutase
- SQUID:
-
Superconducting quantum interference detector
- T2D:
-
Type 2 depleted laccase
- TT2D:
-
Treated type 2 depleted laccase
- UV:
-
Ultraviolet
- VIS:
-
Visible
VII. References
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LuBien, C. D., Solomon, E. I., Spira, D. J., Thamann, T. J., Winkler, M. E.: manuscript in preparation
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Solomon, E.I., Penfield, K.W., Wilcox, D.E. (1983). Active sites in copper proteins an electronic structure overview. In: Copper, Molybdenum, and Vanadium in Biological Systems. Structure and Bonding, vol 53. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0111302
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