Low Temperature 65 Cu NMR Spectroscopy of the Cu+ Site in Azurin
Copper is a ubiquitous component of living systems. It fulfills a vital role in many enzymes, particularly redox enzymes, and more generally in electron transfer. As might be anticipated from the chemistry of the element, the primary redox couple involved in biological redox processes is Cu+/ Cu2+. However, multinuclear copper centers1,2 and mixed metal centers3 give it the ability to participate in multielectron processes. Copper sites in proteins have been classified into several types: type-14 , type-25 , and type-31 copper, as well as the dinuclear CuA center6. Among the best studied are the type-1 sites, characterized by a strong absorbtion in the orange region of the visible spectrum. The blue copper proteins, a class of relatively small, one-electron transfer proteins found in bacteria and plants, notably employs type-1 copper sites.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 970359
- Report Number(s):
- PNNL-SA-63130; JACSAT; 25685; KP1704020; TRN: US201003%%522
- Journal Information:
- Journal of the American Chemical Society, 131(39):13992-13999, Vol. 131, Issue 39; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- English
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