IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex
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چکیده
منابع مشابه
Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe–2S] cluster
Glutaredoxins (Grxs) constitute a superfamily of proteins that perform diverse biological functions. The Saccharomyces cerevisiae glutaredoxin Grx6 not only serves as a glutathione (GSH)-dependent oxidoreductase and as a GSH transferase, but also as an essential [2Fe-2S]-binding protein. Here, the dimeric structure of the C-terminal domain of Grx6 (holo Grx6C), bridged by one [2Fe-2S] cluster c...
متن کامل[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis.
Monothiol glutaredoxins play a crucial role in iron-sulfur (Fe/S) protein biogenesis. Essentially all of them can coordinate a [2Fe-2S] cluster and have been proposed to mediate the transfer of [2Fe-2S] clusters from scaffold proteins to target apo proteins, possibly by acting as cluster transfer proteins. The molecular basis of [2Fe-2S] cluster transfer from monothiol glutaredoxins to target p...
متن کاملElectron Spin Relaxations in Biological [2Fe-2S] Cluster System
The phase coherence relaxation times as long as T2 ∼ 830 − 1030 ± 20 ns were measured for the [2Fe-2S] cluster in the intrinsic protein environment. This relaxation corresponds to a relatively long lasting coherence of the low-spin S = 1/2 state. For this biological cluster, the phase coherence relaxation time was significantly affected by the nuclear hyperfine interactions of N with I = 1. Aft...
متن کاملThe human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation
Members of the bacterial and mitochondrial iron-sulfur cluster (ISC) assembly machinery include the so-called A-type ISC proteins, which support the assembly of a subset of Fe/S apoproteins. The human genome encodes two A-type proteins, termed ISCA1 and ISCA2, which are related to Saccharomyces cerevisiae Isa1 and Isa2, respectively. An additional protein, Iba57, physically interacts with Isa1 ...
متن کاملInvestigating the function of [2Fe–2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential
NADH:quinone oxidoreductase (complex I) couples NADH oxidation and quinone reduction to proton translocation across an energy-transducing membrane. All complexes I contain a flavin to oxidize NADH, seven iron-sulfur clusters to transfer electrons from the flavin to quinone and an eighth cluster (N1a) on the opposite side of the flavin. The role of cluster N1a is unknown, but Escherichia coli co...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2018
ISSN: 0002-7863,1520-5126
DOI: 10.1021/jacs.8b09061