期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 11, 期 3, 页码 261-271出版社
SPRINGER
DOI: 10.1007/s00775-006-0078-9
关键词
copper proteins; thiolate; sulfide; nitric oxide; dioxygen
资金
- NIGMS NIH HHS [GM47365] Funding Source: Medline
The results of studies performed in the author's laboratory are surveyed, with particular emphasis on demonstrating the value of a multidisciplinary synthetic modeling approach for discovering new and unusual chemistry helpful for understanding the properties of the active sites of copper proteins or assessing the feasibility of mechanistic pathways they might follow during catalysis. The discussion focuses on the progress made to date toward comprehending the nitrite reductase catalytic site and mechanism, the electronic structures of copper thiolate electron transfer centers, the sulfido-bridged Cu-Z site in nitrous oxide reductase, and the processes of dioxygen binding and activation by mono- and dicopper centers in oxidases and oxygenases.
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