Rebinding dynamics of CO to Guanidine HC1-denatured heme proteins

Jaeheung Park, JooYoung Kim, T. Lee, M. Lim
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Abstract

Rebinding dynamics of CO photolyzed from GdnHCl-denatured HbCO and MbCO in D20 at 283K was probed by femtosecond mid-IR spectroscopy. The rebinding of CO to the denatured protein is much more efficient and faster than that to the native protein, suggesting that native structure is crucial for efficient expulsion of toxic CO.
一氧化碳与胍hc1变性血红素蛋白的再结合动力学
用飞秒中红外光谱研究了gdnhcl -变性HbCO和MbCO在D20中283K下的再结合动力学。CO与变性蛋白的再结合比与天然蛋白的再结合效率高得多,速度也快得多,这表明天然结构对有效排出有毒CO至关重要。
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