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Temperature-dependent heme kinetics with nonexponential binding and barrier relaxation in the absence of protein conformational substates
We present temperature-dependent kinetic measurements of ultrafast diatomic ligand binding to the “bare” protoheme (L(1)-FePPIX-L(2), where L(1) = H(2)O or 2-methyl imidazole and L(2) = CO or NO). We found that the binding of CO is temperature-dependent and nonexponential over many decades in time,...
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| Autores principales: | , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
National Academy of Sciences
2007
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1976205/ https://ncbi.nlm.nih.gov/pubmed/17804802 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0702622104 |
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