ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster

Jeoung, JH; Dobbek, H

HERO ID

4736529

Reference Type

Journal Article

Year

2018

Language

English

PMID

29507223

HERO ID 4736529
In Press No
Year 2018
Title ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster
Authors Jeoung, JH; Dobbek, H
Journal Proceedings of the National Academy of Sciences of the United States of America
Volume 115
Issue 12
Page Numbers 2994-2999
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 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.
Doi 10.1073/pnas.1720489115
Pmid 29507223
Wosid WOS:000427829500060
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English