期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2018
卷号：115
期号：12
页码：2994-2999
DOI：10.1073/pnas.1720489115
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Chemically demanding reductive conversions in biology, such as the reduction of dinitrogen to ammonia or the Birch-type reduction of aromatic compounds, depend on Fe/S-cluster–containing ATPases. These reductions are typically catalyzed by two-component systems, in which an Fe/S-cluster–containing ATPase energizes an electron to reduce a metal site on the acceptor protein that drives the reductive reaction. Here, we show a two-component system featuring a double-cubane [Fe8S9]-cluster [{Fe4S4(SCys)3}2( μ 2-S)]. The double-cubane–cluster-containing enzyme is capable of reducing small molecules, such as acetylene (C2H2), azide (N3−), and hydrazine (N2H4). We thus present a class of metalloenzymes akin in fold, metal clusters, and reactivity to nitrogenases.
关键词：Fe/S-cluster ; nitrogenase ; acetylene ; ATPase ; electron transfer
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