The Two-State Issue in the Mixed-Valence Binuclear CuA Center in Cytochrome c Oxidase and N2O Reductase
Author:
Affiliation:
1. Department of Chemistry, Stanford University, 333 Campus Drive, Stanford, California 94305, and Division of Biology, The Scripps Research Institute, La Jolla, California 92037
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja067583i
Reference19 articles.
1. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
2. Revisiting the Catalytic CuZ Cluster of Nitrous Oxide (N2O) Reductase
3. A Thiolate-Bridged, Fully Delocalized Mixed-Valence Dicopper(I,II) Complex That Models the CuA Biological Electron-Transfer Site
4. Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for copper-processing and properties of the deduced products, including a new member of the family of ATP/GTP-binding proteins
5. Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase.
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