Solomon E I, Zhou J, Neese F, Pavel E G
Department of Chemistry, Stanford University, Standford, CA 94805, USA.
Chem Biol. 1997 Nov;4(11):795-808. doi: 10.1016/s1074-5521(97)90113-7.
Spectroscopic properties of the redox-active iron in the active site of plant and mammalian lipoxygenases can now be combined with recent crystal structure determinations to obtain new insights into lipoxygenase reaction mechanisms.
植物和哺乳动物脂氧合酶活性位点中氧化还原活性铁的光谱性质，现在可以与最近的晶体结构测定结果相结合，从而获得对脂氧合酶反应机制的新见解。
