An Undergraduate Laboratory Experiment in Bioinorganic Chemistry: Ligation States of Myoglobin
An Undergraduate Laboratory Experiment in Bioinorganic Chemistry: Ligation States of Myoglobin
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DOI：
10.1021/ed100600c
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发表时间：
2011-07-01
影响因子：
3
通讯作者：
Bailey, James A.
中科院分区：
文献类型：
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作者：
Bailey, James A.
虽然有许多无机模型系统，很容易作为本科生实验室实验在生物无机化学，有几个例子，探索实际的生物分子的无机化学。我们提出了一个实验室实验，使用氧结合蛋白肌红蛋白，可以很容易地纳入本科实验室课程。这个高度直观的实验中，一氧化碳和分子氧的配体结合反应是使用扫描可见吸收光谱监测提供了机会，以研究O（2）和CO的相对结合强度的还原铁卟啉中心。这一过程是呼吸机制的重要的第一步，也是讨论几个有趣主题的一个方便的切入点，包括，例如，金属在生物学中的作用;金属卟啉中的配体结合和氧化还原状态;光谱探针在动力学和机制研究中的应用;蛋白质动力学;和结构功能关系。
Although there are numerous inorganic model systems that are readily presented as undergraduate laboratory experiments in bioinorganic chemistry, there are few examples that explore the inorganic chemistry of actual biological molecules. We present a laboratory experiment using the oxygen-binding protein myoglobin that can be easily incorporated into an undergraduate laboratory course. This highly intuitive experiment in which ligand-binding reactions of carbon monoxide and dioxygen are monitored using scanning visible absorption spectroscopy provides the opportunity to investigate the relative binding strengths of O(2) and CO to the reduced iron porphyrin center. This process represents an important first step in the mechanism of respiration and oilers a convenient entry point into several interesting topics for discussion including, for example, the role of metals in biology; ligand binding and redox states in metalloporphyrins; the application of spectroscopic probes to the study of kinetics and mechanism; protein dynamics; and structure function relationships.