Evidence for non-cysteinyl coordination of the [2Fe-2S] cluster inEscherichia colisuccinate dehydrogenase
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چکیده
منابع مشابه
[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 کاملMolybdenum EXAFS of the Desulfovibrio gigas Mo(2Fe-2S) protein--structural similarity to "desulfo" xanthine dehydrogenase.
The molybdenum EXAFS of the Mo(2Fe-2S) protein from Desulfovibrio gigas has been examined using fluorescence detection and synchrotron radiation. In the oxidized form the molybdenum environment is found to contain two terminal oxo groups and two long (2.47 A) Mo-S bonds. Evidence was also found for an oxygen or nitrogen donor ligand at 1.90 A. Addition of dithionite to the oxidized enzyme resul...
متن کاملBinding of histidine in the (Cys)3(His)1-coordinated [2Fe-2S] cluster of human mitoNEET.
Human mitoNEET is a homodimeric iron-sulfur protein located in the outer mitochondrial membrane with unknown function, but which is known to interact with thiazolidinedione diabetes drugs. Each monomer houses a [2Fe-2S] cluster with an unusual (Cys)(3)(His)(1) ligation. The His ligand is important for enabling cluster release and for tuning the redox potential. We use multifrequency (X-, Ka-, a...
متن کاملStructure-function studies of [2Fe-2S] ferredoxins.
The ability to overexpress [2Fe-2S] ferredoxins in Escherichia coli has opened up exciting research opportunities. High-resolution x-ray structures have been determined for the wild-type ferredoxins produced by the vegatative and heterocyst forms of Anabaena strain 7120 (in their oxidized states), and these have been compared to structural information derived from multidimensional, multinuclear...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1992
ISSN: 0014-5793
DOI: 10.1016/0014-5793(92)80086-v