ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster
Journal article
Abstract
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(μ2-S)]. The doublecubane- 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.
Publication Details
Author list: Jeoung J., Dobbek H.
Journal: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Publication year: 2018
Volume number: 115
Issue number: 12
Pages: 2994-2999
ISSN: 0027-8424
URL: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85044333633&origin=inward
Languages: English-Great Britain
