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Ligand Access to the Active Site in Thermus thermophilus ba(3) and Bovine Heart aa(3) Cytochrome Oxidases

Knowledge of the structure and dynamics of the ligand channel(s) in heme-copper oxidases is critical for understanding how the protein environment modulates their functions. Using photolabile NO and O(2) carriers, we recently found that NO and O(2) binding in Thermus thermophilus ba(3) (Tt ba(3)) is...

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Autors principals: McDonald, William, Funatogawa, Chie, Li, Yang, Szundi, Istvan, Chen, Ying, Fee, James A., Stout, C. David, Einarsdóttir, Ólöf
Format: Artigo
Idioma:Inglês
Publicat: 2013
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC3569493/
https://ncbi.nlm.nih.gov/pubmed/23282175
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi301358a
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