ArticleInorganic chemistry2013
Generation of high-spin iron(I) in a protein environment using cryoreduction.
Article in Inorganic chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 15 citations in OpenAlex.
- Repurposing metalloproteins as mimics of natural metalloenzymes for small-molecule activation.Journal of inorganic biochemistry · 2021Review
- Light-Activated Electron Transfer and Catalytic Mechanism of Carnitine Oxidation by Rieske-Type Oxygenase from Human Microbiota.Angewandte Chemie (International ed. in English) · 2021Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
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Abstract
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.
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