Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures

Beinert, Helmut; Holm, R. H.; Münck, Eckard

doi:10.1126/science.277.5326.653

Cited by 1,780 publications

(1,656 citation statements)

References 69 publications

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“…clusters [24,25] and reveals a unique valence localization-to-delocalization transition due to electron hopping. Such a localization-to-delocalization transition of the merging type has not been observed in physiological protein-bound [2Fe-2S] clusters, but has been observed only in a few synthetic model compounds with mixed-valence [2Fe-2S] cores [40].…”

Section: Reduced Fl Constructmentioning

confidence: 99%

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

et al. 2013

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The eukaryotic anamorsin protein family, which has recently been proposed to be part of an electron transfer chain functioning in the early steps of cytosolic iron-sulfur (Fe/S) protein biogenesis, is characterized by a largely unstructured domain (CIAPIN1) containing two conserved cysteine-rich motifs (CX 8 CX 2 CXC and CX 2 CX 7 CX 2 C) whose Fe/S binding properties and electronic structures are not well defined. Here, we found that (1) each motif in human anamorsin is able to bind independently a [2Fe-2S] cluster through its four cysteine residues, the binding of one cluster mutually excluding the binding of the second, (2) the reduced [2Fe-2S] ? clusters exhibit a unique electronic structure with considerable anisotropy in their coordination environment, different from that observed in reduced, plant-type and vertebratetype [2Fe-2S] ferredoxin centers, (3) the reduced cluster bound to the CX 2 CX 7 CX 2 C motif reveals an unprecedented valence localization-to-delocalization transition as a function of temperature, and (4) only the [2Fe-2S] cluster bound to the CX 8 CX 2 CXC motif is involved in the electron transfer with its physiological protein partner Ndor1. The unique electronic properties of both [2Fe-2S] centers can be interpreted by considering that both cysteine-rich motifs are located in a highly unstructured and flexible protein region, whose local conformational heterogeneity can induce anisotropy in metal coordination. This study contributes to the understanding of the functional role of the CIAPIN1 domain in the anamorsin family, suggesting that only the [2Fe-2S] cluster bound to the CX 8 CX 2 CXC motif is indispensable in the electron transfer chain assembling cytosolic Fe/S proteins.

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Section: Reduced Fl Constructmentioning

confidence: 99%

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

et al. 2013

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“…Iron-sulfur (Fe/S) clusters are ubiquitous inorganic cofactors that are present in all forms of life 1 . Despite the chemical simplicity of Fe/S clusters, their biosynthesis and insertion into apoproteins within cells require dedicated and complex machinery 2,3 .…”

Section: Introductionmentioning

confidence: 99%

Analysis of iron–sulfur protein maturation in eukaryotes

2009

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“…The iron-sulfur clusters bound in Fds are , , and [2Fe-2S] (Beinert et al 1997). In some cyanobacteria and heterotrophic bacteria, flavodoxins are able to functionally replace Fd.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

2004

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From Bacillus subtilis cell extracts, ferredoxin-NADP + reductase (FNR) was purified to homogeneity and found to be the yumC gene product by N-terminal amino acid sequencing. YumC is a ~94 kDa homodimeric protein with one molecule of non-covalently bound FAD per subunit. In a diaphorase assay with 2,6-dichlorophenol-indophenol as an electron acceptor, the affinity to NADPH was much higher than to NADH, with K m values of 0.57 vs. >200 µM. K cat values of YumC with NADPH were 22.7 and 35.4 s -1 in diaphorase and in a ferredoxin-dependent NADPH-cytochrome c reduction assay, respectively. The cell extracts contained another diaphorase-active enzyme, the yfkO gene product, but its affinity for ferredoxin was very low. The deduced YumC amino acid sequence has high identity to that of the recently identified Chlorobium tepidum FNR. A genomic database search indicated that there are more than 20 genes encoding proteins that share a high level of amino acid sequence identity with YumC and annotated variously as NADH oxidase, thioredoxin reductase, thioredoxin reductase-like protein, etc. These genes are found notably in Gram-positive bacteria except for Clostridia, and less frequently in archaea and proteobacteria. We propose that YumC and C. tepidum FNR constitute a new group of FNR which should be added to the already established plant type, bacteria type, and mitochondria type FNR groups.

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Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures

Cited by 1,780 publications

References 69 publications

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

Analysis of iron–sulfur protein maturation in eukaryotes

Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

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