2022
DOI: 10.1021/jacs.2c09480
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Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster

Abstract: Nitrogenase catalyzes the multielectron reduction of dinitrogen to ammonia. Electron transfer in the catalytic protein (MoFeP) proceeds through a unique [8Fe-7S] cluster (P-cluster) to the active site (FeMoco). In the reduced, all-ferrous (P N ) state, the P-cluster is coordinated by six cysteine residues. Upon twoelectron oxidation to the P 2+ state, the P-cluster undergoes conformational changes in which a highly conserved oxygen-based residue (a Ser or a Tyr) and a backbone amide additionally ligate the clu… Show more

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Cited by 3 publications
(3 citation statements)
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“…Tyr as a [4Fe-4S] cluster coordination residue, to the best of our knowledge, has only been demonstrated in the hydrogenase maturase HydE . However, in the case of nitrogenase, oxidation of the p-cluster elicits a conformational change where a highly conserved oxygen-based residue (Ser/or, in some cases, Tyr) and a backbone amide coordinate the cluster, which has been hypothesized to play a protective role against oxidative stress and act as a redox switch . We propose that tyrosine plays a similar role in TigE, protecting the more exposed Aux I cluster from oxidative stress (Figure S9) and acting as a redox switch.…”
Section: Discussionmentioning
confidence: 92%
See 1 more Smart Citation
“…Tyr as a [4Fe-4S] cluster coordination residue, to the best of our knowledge, has only been demonstrated in the hydrogenase maturase HydE . However, in the case of nitrogenase, oxidation of the p-cluster elicits a conformational change where a highly conserved oxygen-based residue (Ser/or, in some cases, Tyr) and a backbone amide coordinate the cluster, which has been hypothesized to play a protective role against oxidative stress and act as a redox switch . We propose that tyrosine plays a similar role in TigE, protecting the more exposed Aux I cluster from oxidative stress (Figure S9) and acting as a redox switch.…”
Section: Discussionmentioning
confidence: 92%
“…42 However, in the case of nitrogenase, oxidation of the p-cluster elicits a conformational change where a highly conserved oxygen-based residue (Ser/or, in some cases, Tyr) and a backbone amide coordinate the cluster, which has been hypothesized to play a protective role against oxidative stress and act as a redox switch. 43 We propose that tyrosine plays a similar role in TigE, protecting the more exposed Aux I cluster from oxidative stress (Figure S9) and acting as a redox switch. However, based on our activity data, the role of tyrosine as a redox switch is more likely.…”
Section: ■ Conclusionmentioning
confidence: 89%
“…An intriguing aspect of the P-cluster is that some substitutions, or even deletions, of the cluster cysteine ligands can be generated that are still able to grow diazotrophically, including substitutions at α-Cys88 that bridges the two subclusters [84,85]. Structures from the Tezcan group [86][87][88] of point mutations in the oxygenic residues surrounding the P-cluster demonstrated that the cluster could become compositionally labile upon oxidation and lose Fe centers while still retaining near wild-type levels reduction of nitrogen. Based on these observations, the authors proposed that inherent lability of the P-cluster may play a role in catalysis.…”
Section: Proton Coupled Electron Transfer To the Nitrogenase Metalloc...mentioning
confidence: 99%