2019
DOI: 10.1016/j.redox.2019.101296
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A conserved motif liganding the [4Fe–4S] cluster in [4Fe–4S] fumarases prevents irreversible inactivation of the enzyme during hydrogen peroxide stress

Abstract: Organisms have evolved two different classes of the ubiquitous enzyme fumarase: the [4Fe–4S] cluster-containing class I enzymes are oxidant-sensitive, whereas the class II enzymes are iron-free and therefore oxidant-resistant. When hydrogen peroxide (H2O2) attacks the most-studied [4Fe–4S] fumarases, only the cluster is damaged, and thus the cell can rapidly repair the enzyme. However, this study shows that when elevated levels of H2O2 oxidized the class I fumarase of the obligate anaerobe Bacteroides thetaiot… Show more

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Cited by 24 publications
(17 citation statements)
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“…The acid-labile sulfur, including Fe-S clusters, is sulfide [ 52 , 53 ]. When O 2 •− and HO• oxidize Fe-S clusters and release Fe 2+ [ 54 , 55 , 56 ], the sulfur in the cluster is theoretically oxidized to sulfane sulfur (zero valences), as sulfide reacts with ROS to produce sulfane sulfur [ 57 ]. H 2 O 2 and tBH were unable to increase iSS ( Figure 7 A), perhaps partly because they are rapidly metabolized by E. coli cells [ 58 ], partly because they react with sulfane sulfur at a relatively slow rate [ 40 ], and partly because they do not directly damage Fe-S clusters [ 59 ].…”
Section: Discussionmentioning
confidence: 99%
“…The acid-labile sulfur, including Fe-S clusters, is sulfide [ 52 , 53 ]. When O 2 •− and HO• oxidize Fe-S clusters and release Fe 2+ [ 54 , 55 , 56 ], the sulfur in the cluster is theoretically oxidized to sulfane sulfur (zero valences), as sulfide reacts with ROS to produce sulfane sulfur [ 57 ]. H 2 O 2 and tBH were unable to increase iSS ( Figure 7 A), perhaps partly because they are rapidly metabolized by E. coli cells [ 58 ], partly because they react with sulfane sulfur at a relatively slow rate [ 40 ], and partly because they do not directly damage Fe-S clusters [ 59 ].…”
Section: Discussionmentioning
confidence: 99%
“…However, myriocin pre-treatment significantly suppressed ROS production under glutathione depletion. Additionally, the level of LIP was also decreased, most likely due to the less ROS which leads to the releasement of iron from its storage proteins ( Di Tano et al., 2020 ; Lu and Imlay, 2019 ; Torti and Torti, 2013 ). Unlike GPx4 or FSP1, the protective role of myriocin against ferroptosis relies on the prevention of lipid peroxide accumulation caused by the oxidative reaction of polyunsaturated fatty acid with ROS and iron ( Boada-Romero et al., 2020 ; Tang et al., 2019 ).…”
Section: Discussionmentioning
confidence: 99%
“…The radicals NO and ● OH can bind to Fe atoms of the Fe–S clusters [ 104 ]. ROS, mainly superoxide (O 2 − ), can oxidize Fe–S clusters starting with an iron release, promoting cluster instability and slow degradation leading to irreversible damage to the protein backbone of a particular enzyme [ 105 ]. Therefore, enzymes that undergo prolonged exposure to oxidative stress show a poor prognosis for renewal [ 106 ].…”
Section: Repair Of Damaged Fe–s Clustersmentioning
confidence: 99%
“…Bruska et al performed detailed studies of a different kind of ROS–Fe–S cluster interaction [ 104 ]. Most Fe–S proteins hide the vulnerable cluster inside the polypeptide chain; however, some of them require direct involvement of the cluster to perform their activity [ 105 ]. Such exposed clusters, mainly [4Fe–4S] forms, are more prone to oxidative stress [ 107 ].…”
Section: Repair Of Damaged Fe–s Clustersmentioning
confidence: 99%
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