利用低温还原法在蛋白质环境中生成高自旋铁（I）
Generation of high-spin iron(I) in a protein environment using cryoreduction.
机构信息
Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA.
出版信息
Inorg Chem. 2013 Jul 1;52(13):7323-5. doi: 10.1021/ic4011339. Epub 2013 Jun 10.
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.
高自旋 Fe(1+) 位点在铁硫蛋白中具有重要意义，但在合成化合物中很少见，在金属蛋白中也未知。在这里，我们展示了一个在蛋白质环境中具有高自旋非血红素 Fe(1+)的光谱特征实例。用 (60)Co γ 辐射将 Fe(2+)-取代的蓝铜蛋白在 77 K 下还原，生成一个具有 S = (3)/2（高自旋）Fe(1+)中心的新物种，该中心具有 D > 0 和 E/D ~ 0.25。这种瞬态物种在甘油-水玻璃中仅在 ~170 K 以下稳定。电子顺磁共振和穆斯堡尔光谱学的组合为在蛋白质支架中识别瞬态高自旋 Fe(1+) 位点提供了一种强大的手段。
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