Frauenfelder H, McMahon B H, Austin R H, Chu K, Groves J T
Center for Nonlinear Studies, MS-B 258, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2370-4. doi: 10.1073/pnas.041614298. Epub 2001 Feb 20.
The grail of protein science is the connection between structure and function. For myoglobin (Mb) this goal is close. Described as only a passive dioxygen storage protein in texts, we argue here that Mb is actually an allosteric enzyme that can catalyze reactions among small molecules. Studies of the structural, spectroscopic, and kinetic properties of Mb lead to a model that relates structure, energy landscape, dynamics, and function. Mb functions as a miniature chemical reactor, concentrating and orienting diatomic molecules such as NO, CO, O(2), and H(2)O(2) in highly conserved internal cavities. Reactions can be controlled because Mb exists in distinct taxonomic substates with different catalytic properties and connectivities of internal cavities.
蛋白质科学的圣杯是结构与功能之间的联系。对于肌红蛋白（Mb）而言，这一目标已近在咫尺。在教科书中，Mb仅被描述为一种被动的双氧气储存蛋白，但我们在此认为，Mb实际上是一种能催化小分子间反应的别构酶。对Mb的结构、光谱和动力学性质的研究得出了一个将结构、能量景观、动力学和功能联系起来的模型。Mb起着微型化学反应器的作用，在高度保守的内部腔室中浓缩并定向诸如NO、CO、O₂和H₂O₂等双原子分子。反应能够得到控制，因为Mb以具有不同催化特性和内部腔室连通性的不同分类亚状态存在。
