期刊
SCIENCE
卷 299, 期 5609, 页码 1039-1042出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1078020
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资金
- NIGMS NIH HHS [GM62904, GM29909] Funding Source: Medline
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.
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