X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe
            <sub>4</sub>
            S
            <sub>4</sub>
            clusters

Nicolet, Yvain; Rohac, Roman; Martin, Lydie; Fontecilla‐Camps, J.C.

doi:10.1073/pnas.1302388110

Cited by 59 publications

(59 citation statements)

References 34 publications

(40 reference statements)

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“…This implies that apo-IRP1 left after ROS-or NO-mediated Fe-S extrusion is different from the neosynthesized form. As outlined previously, protein-bound [4Fe-4S] display noticeable modifications in the Fe-S binding site upon oxygen-mediated Fe-S disassembly, notably persulfuration (67)(68)(69). Therefore, we speculate that cysteine persulfuration on apo-IRP1 following exposure to oxygen or nitrogen species favors mNT Fe-S delivery.…”

Section: Discussionmentioning

confidence: 90%

The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase/Iron Regulatory Protein 1

Ferecatu

Gonçalves

Golinelli-Cohen

et al. 2014

Journal of Biological Chemistry

124

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Background:MitoNEET is a mammalian iron-sulfur protein with the ability to transfer iron-sulfur (Fe-S) in vitro. Results: MitoNEET conveys Fe-S from the mitochondrion to the cytosol and reactivates cytosolic iron regulatory protein 1 into an Fe-S aconitase. Conclusion: A novel mitoNEET-dependent Fe-S repair pathway affects a key regulator of iron metabolism. Significance: MitoNEET is the first mitochondrial protein found to be involved in mammalian cytosolic Fe-S repair.

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Section: Discussionmentioning

confidence: 90%

The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase/Iron Regulatory Protein 1

Ferecatu

Gonçalves

Golinelli-Cohen

et al. 2014

Journal of Biological Chemistry

124

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“…Multiple X-ray crystal structures of HydE exist and these include SAM and 5′-deoxyadenosine/methionine bound states [263][264][265]. The global architecture of HydE shows the existence of an internal electropositive cavity spanning the breadth of the (βα) 8 TIM barrel fold.…”

Section: An Undefined Role In H-cluster Biosynthesis: Hydementioning

confidence: 98%

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Peters

Schut

Boyd

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

397

374

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The [FeFe]- and [NiFe]-hydrogenases catalyze the formal interconversion between hydrogen and protons and electrons, possess characteristic non-protein ligands at their catalytic sites and thus share common mechanistic features. Despite the similarities between these two types of hydrogenases, they clearly have distinct evolutionary origins and likely emerged from different selective pressures. [FeFe]-hydrogenases are widely distributed in fermentative anaerobic microorganisms and likely evolved under selective pressure to couple hydrogen production to the recycling of electron carriers that accumulate during anaerobic metabolism. In contrast, many [NiFe]-hydrogenases catalyze hydrogen oxidation as part of energy metabolism and were likely key enzymes in early life and arguably represent the predecessors of modern respiratory metabolism. Although the reversible combination of protons and electrons to generate hydrogen gas is the simplest of chemical reactions, the [FeFe]- and [NiFe]-hydrogenases have distinct mechanisms and differ in the fundamental chemistry associated with proton transfer and control of electron flow that also help to define catalytic bias. A unifying feature of these enzymes is that hydrogen activation itself has been restricted to one solution involving diatomic ligands (carbon monoxide and cyanide) bound to an Fe ion. On the other hand, and quite remarkably, the biosynthetic mechanisms to produce these ligands are exclusive to each type of enzyme. Furthermore, these mechanisms represent two independent solutions to the formation of complex bioinorganic active sites for catalyzing the simplest of chemical reactions, reversible hydrogen oxidation. As such, the [FeFe]- and [NiFe]-hydrogenases are arguably the most profound case of convergent evolution. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.

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“…In (16,17). Similarly, liquid chromatography mass spectrometry (LC-MS) experiments showed that multiple cysteine persulfides [RS(S) n , where n = 1-4] were formed during the FNR reaction time course (16).…”

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confidence: 99%

Mass spectrometric identification of intermediates in the O ₂ -driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR

Crack

Thomson

Brun

2017

Proc. Natl. Acad. Sci. U.S.A.

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The iron-sulfur cluster containing protein Fumarate and Nitrate Reduction (FNR) is the master regulator for the switch between anaerobic and aerobic respiration in and many other bacteria. The [4Fe-4S] cluster functions as the sensory module, undergoing reaction with O that leads to conversion to a [2Fe-2S] form with loss of high-affinity DNA binding. Here, we report studies of the FNR cluster conversion reaction using time-resolved electrospray ionization mass spectrometry. The data provide insight into the reaction, permitting the detection of cluster conversion intermediates and products, including a [3Fe-3S] cluster and persulfide-coordinated [2Fe-2S] clusters [[2Fe-2S](S) , where = 1 or 2]. Analysis of kinetic data revealed a branched mechanism in which cluster sulfide oxidation occurs in parallel with cluster conversion and not as a subsequent, secondary reaction to generate [2Fe-2S](S) species. This methodology shows great potential for broad application to studies of protein cofactor-small molecule interactions.

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X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe ₄ S ₄ clusters

Cited by 59 publications

References 34 publications

The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase/Iron Regulatory Protein 1

The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase/Iron Regulatory Protein 1

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Mass spectrometric identification of intermediates in the O ₂ -driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR

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X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe 4 S 4 clusters

Cited by 59 publications

References 34 publications

The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase/Iron Regulatory Protein 1

The Diabetes Drug Target MitoNEET Governs a Novel Trafficking Pathway to Rebuild an Fe-S Cluster into Cytosolic Aconitase/Iron Regulatory Protein 1

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Mass spectrometric identification of intermediates in the O 2 -driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR

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X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe ₄ S ₄ clusters

Mass spectrometric identification of intermediates in the O ₂ -driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR