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Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E(2)(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis
[Image: see text] Early studies in which nitrogenase was freeze-trapped during enzymatic turnover revealed the presence of high-spin (S = (3)/(2)) electron paramagnetic resonance (EPR) signals from the active-site FeMo-cofactor (FeMo-co) in electron-reduced intermediates of the MoFe protein. Histori...
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| Опубликовано в: : | Inorg Chem |
|---|---|
| Главные авторы: | , , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American
Chemical Society
2018
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| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6008734/ https://ncbi.nlm.nih.gov/pubmed/29575898 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.inorgchem.8b00271 |
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