The Characterization of Lipoxygenase Iron

脂氧合酶是一种独特的非血红素铁双加氧酶。它最先在豆科植物的种子中被观察到，因为它在种子中相对丰富，并且能够进行某些容易观察到的催化转化。尽管如此，这些来源的酶的生理作用一直很难确定。最近有证据表明，脂肪氧合酶参与植物生长发育的两个阶段，即萌发和衰老，近年来哺乳动物脂肪氧合酶的发现导致了对该酶的研究的复兴。芬克博士正试图描述这种酶的一种成分结构，这种结构与其提出的作用机制密切相关。虽然非血红素铁被认为在脂氧合酶催化活性的表达中起关键作用，但人们对蛋白质中原子的结合部位知之甚少。铁位置的结构将通过穆斯堡尔光谱进行研究，穆斯堡尔光谱是一种对蛋白质中金属的电子环境具有独特选择性的探测器。为了确认其他技术揭示的结构特征，还将用X射线吸收光谱研究铁的位置。

Lipoxygenase is a distinctive non-heme iron dioxygenase. It was first observed in the seeds of leguminous plants because of its relative abundance there and its ability to carry out certain easily observed catalytic transformations. In spite of this, a physiological role for the enzyme from these sources has been difficult to pinpoint. Evidence that lipoxygenases are involved in two stages of plant growth and development, germination and senescence, has been recently presented and the discovery of mammalian lipoxygenases has led in recent years to a renaissance in investigations of the enzyme. Dr. Funk is trying to characterize a component structure of the enzyme that is critically related to its proposed mechanism of action. While non-heme iron is believed to play a key role in the expression of catalytic activity of lipoxygenase, very little is known about the binding site for the atom in the protein. The structure of the iron site will be studied by Mossbauer spectroscopy, a uniquely selective probe of the electronic environment of metals in proteins. The iron site will also be investigated by X-ray absorption spectroscopy in order to provide confirmation of the structural features revealed by other techniques.