Structural basis for coupled ATP-driven electron transfer in the double-cubane cluster protein

Jeoung, Jae‐Hun; Nicklisch, Sabine; Dobbek, Holger

doi:10.1073/pnas.2203576119

Cited by 5 publications

(3 citation statements)

References 46 publications

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Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

“…Additionally, more complex clusters can be formed by combining the basic clusters together. For the most part, these complex FeS clusters are found in nitrogenases (Figure 2, right) [40][41][42]. The transition metal iron is key to one of the main underlying functions of FeS clusters, the ability to accommodate reversible binding of a single electron and to enhance the movement of single, unpaired electrons through a relay system, such as that found in the respiratory complex I [43].…”

Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

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Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

SantaMaria,

Rouault

2024

Inorganics

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Iron is an essential nutrient and necessary for biological functions from DNA replication and repair to transcriptional regulation, mitochondrial respiration, electron transfer, oxygen transport, photosynthesis, enzymatic catalysis, and nitrogen fixation. However, due to iron’s propensity to generate toxic radicals which can cause damage to DNA, proteins, and lipids, multiple processes regulate the uptake and distribution of iron in living systems. Understanding how intracellular iron metabolism is optimized and how iron is utilized to regulate other intracellular processes is important to our overall understanding of a multitude of biological processes. One of the tools that the cell utilizes to regulate a multitude of functions is the ligation of the iron–sulfur (Fe-S) cluster cofactor. Fe-S clusters comprised of iron and inorganic sulfur are ancient components of living matter on earth that are integral for physiological function in all domains of life. FeS clusters that function as biological sensors have been implicated in a diverse group of life from mammals to bacteria, fungi, plants, and archaea. Here, we will explore the ways in which cells and organisms utilize Fe-S clusters to sense changes in their intracellular environment and restore equilibrium.

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Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

Section: Fes Cluster Structure Geometries and Biogenesismentioning

confidence: 99%

Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

SantaMaria,

Rouault

2024

Inorganics

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“…The homohexameric enzyme (Mr 359 kDa) was prepared from T. chlorobenzoica 3CB-1 strain [21]. The doublecubane cluster protein (WP_235551353, DCCP) catalyzes the reduction of inert substrates like acetylene, but its physiological function is unknown [22]. The homodimeric enzyme (Mr 95 kDa) was isolated from Moorella thermoacetica DSM 521 (growth temperature of 50 • C).…”

Section: Applied Proteinsmentioning

confidence: 99%

Ethoxylate Polymer-Based 96-Well Screen for Protein Crystallization

Demmer,

Lemaire,

Belhamri

et al. 2023

Crystals

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Crystallization is the limiting step in X-ray structure determination of biological macromolecules. As crystallization experiments can be largely automatized, the diversity of precipitant solutions is often the determinant factor to obtain crystals of high quality. Here, we introduce a 96-well screening kit of crystallization conditions, centered on three ethoxylate-based organic polymers as precipitants and various additional compounds to promote crystal formation. This crystallization screen was tested on various non-standard proteins from bacteria and archaea. Structure determination succeeded for seven out of thirteen targets based on crystals that frequently diffracted to a higher resolution than those obtained with commercially available screening kits. Crystallization hits were rarely similar among the three ethoxylate-based organic polymers and, in comparison, with already available crystallization screens. Hence, the presented crystallization screen is an efficient tool to complement other screens and increase the likelihood of growing crystals suitable for X-ray structure determination.

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Double Cubane Cluster Protein and Its Reductase

Jeoung,

Dobbek

2024

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Chemically demanding reductions in biology may be achieved by coupling electron transfer to ATP hydrolysis. To achieve a unidirectional electron transfer against a redox‐potential gradient, the double‐cubane cluster‐containing protein (DCCP) forms a complex with an ATP‐dependent reductase, which couples ATP hydrolysis with electron transfer from its [4Fe4S] cluster to the active site of DCCP. DCCP has been named after its cofactor, containing two cubane‐type [4Fe4S] clusters linked by a μ‐sulfido ligand. The double‐cubane cluster is coordinated by six conserved cysteine residues, with both [4Fe4S] subclusters experiencing different environments. While the physiological substrate of DCCP is unknown, it catalyzes the nonphysiological reduction of acetylene, azide, and hydrazine. DCCP and its reductase are homologous to atypical dehydratases and class‐I benzoyl‐CoA reductases and share mechanistic analogies with nitrogenases and reductive activators of corrinoid proteins.

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Structural basis for coupled ATP-driven electron transfer in the double-cubane cluster protein

Cited by 5 publications

References 46 publications

Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

Ethoxylate Polymer-Based 96-Well Screen for Protein Crystallization

Double Cubane Cluster Protein and Its Reductase

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