| Autor: |
Davydov RM; Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA., McLaughlin MP, Bill E, Hoffman BM, Holland PL |
| Jazyk: |
angličtina |
| Zdroj: |
Inorganic chemistry [Inorg Chem] 2013 Jul 01; Vol. 52 (13), pp. 7323-5. Date of Electronic Publication: 2013 Jun 10. |
| DOI: |
10.1021/ic4011339 |
| Abstrakt: |
High-spin Fe(1+) sites are potentially important in iron-sulfur proteins but are rare in synthetic compounds and unknown in metalloproteins. Here, we demonstrate a spectroscopically characterized example of high-spin non-heme Fe(1+) in a protein environment. Cryoreduction of Fe(2+)-substituted azurin at 77 K with (60)Co γ radiation generates a new species with a S = (3)/2 (high-spin) Fe(1+) center having D > 0 and E/D ~ 0.25. This transient species is stable in a glycerol-water glass only up to ~170 K. A combination of electron paramagnetic resonance and Mössbauer spectroscopies provides a powerful means of identifying a transient high-spin Fe(1+) site in a protein scaffold. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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