千禧年的铁螯合酶：结构、机制与[2Fe-2S]簇
Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters.
作者信息
Dailey H A, Dailey T A, Wu C K, Medlock A E, Wang K F, Rose J P, Wang B C
机构信息
Department of Biochemistry and Molecular Biology, University of Georgia, Athens 30605-7229, USA.
出版信息
Cell Mol Life Sci. 2000 Dec;57(13-14):1909-26. doi: 10.1007/pl00000672.
Ferrochelatase (E.C. 4.99.1.1, protoheme ferrolyase) catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme (heme). In the past 2 years, the crystal structures of ferrochelatases from the bacterium Bacillus subtilis and human have been determined. These structures along with years of biophysical and kinetic studies have led to a better understanding of the catalytic mechanism of ferrochelatase. At present, the complete DNA sequences of 45 ferrochelatases from procaryotes and eucaryotes are available. These sequences along with direct protein studies reveal that ferrochelatases, while related, vary significantly in amino acid sequence, molecular size, subunit composition, solubility, and the presence or absence of nitric-oxide-sensitive [2Fe-2S] cluster.
亚铁螯合酶（E.C. 4.99.1.1，原卟啉亚铁裂解酶）催化亚铁插入原卟啉IX中形成原血红素（血红素）。在过去两年中，已测定了来自枯草芽孢杆菌和人类的亚铁螯合酶的晶体结构。这些结构以及多年的生物物理和动力学研究使人们对亚铁螯合酶的催化机制有了更好的理解。目前，可获得来自原核生物和真核生物的45种亚铁螯合酶的完整DNA序列。这些序列以及直接的蛋白质研究表明，亚铁螯合酶虽然相关，但在氨基酸序列、分子大小、亚基组成、溶解度以及是否存在对一氧化氮敏感的[2Fe-2S]簇方面存在显著差异。
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