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Pourbaix diagram, proton-coupled electron transfer and decay kinetics of a protein tryptophan radical: Comparing the redox properties of W(32)· and Y(32)· generated inside the structurally characterized α(3)W and α(3)Y proteins
Protein “hole” hopping typically involves spatially arranged redox-active tryptophan and/or tyrosine residues. Thermodynamic information is scarce for this type of process. The well-structured α(3)W model protein was studied by protein film square wave voltammetry and transient absorption spectrosco...
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| Publicado no: | J Am Chem Soc |
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| Main Authors: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2017
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5762255/ https://ncbi.nlm.nih.gov/pubmed/29190082 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.7b08032 |
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