Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?
Interaction of the two high-spin hemes in the oxygen reduction site of the bd-type quinol oxidase from Escherichia coli has been studied by femtosecond multicolor transient absorption spectroscopy. The previously unidentified Soret band of ferrous heme b(595) was determined to be centered around 440...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2000
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC26473/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10660685/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.030528197 |
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