Interactions of hydrogen sulfide with AhpE from Mycobacterium tuberculosis: formation and reactions of a model peroxiredoxin persulfide

Reyes, Aníbal M.; Cuevasanta, Ernesto; Armas, María Inés De; Mastrogiovanni, Mauricio; Zeida, Ari; Radí, Rafael; Álvarez, Beatriz; Trujillo, Madia

doi:10.1016/j.freeradbiomed.2018.10.107

Cited by 2 publications

(1 citation statement)

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“…First, S-sulfenylation is a reversible oxidative PTM of cysteine thiols, which oxidizes thiols of cysteine into sulfenic acid (R-SOH) groups. Reyes et al used peroxiredoxin alkyl hydroperoxide reductase E of Mycobacterium tuberculosis (MtAhpE-S-) as the research material to confirm that H 2 S could react with MtAhpE-SOH (MtAhpE-S-of S-sulfenylation) to form persulfides (MtAhpE-SS-) [47]. It has also reported that the GAPDH of S-sulfenylation could further react with H 2 S to form persulfides in mammals [48].…”

Section: H 2 S and Protein Persulfidation In Plantsmentioning

confidence: 99%

Protein Persulfidation in Plants: Function and Mechanism

et al. 2021

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As an endogenous gaseous transmitter, the function of hydrogen sulfide (H2S) has been extensively studied in plants. Once synthesized, H2S may be involved in almost all life processes of plants. Among them, a key route for H2S bioactivity occurs via protein persulfidation, in which process oxidizes cysteine thiol (R-SH) groups into persulfide (R-SSH) groups. This process is thought to underpin a myriad of cellular processes in plants linked to growth, development, stress responses, and phytohormone signaling. Multiple lines of emerging evidence suggest that this redox-based reversible post-translational modification can not only serve as a protective mechanism for H2S in oxidative stress, but also control a variety of biochemical processes through the allosteric effect of proteins. Here, we collate emerging evidence showing that H2S-mediated persulfidation modification involves some important biochemical processes such as growth and development, oxidative stress, phytohormone and autophagy. Additionally, the interaction between persulfidation and S-nitrosylation is also discussed. In this work, we provide beneficial clues for further exploration of the molecular mechanism and function of protein persulfidation in plants in the future.

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Section: H 2 S and Protein Persulfidation In Plantsmentioning

confidence: 99%

Protein Persulfidation in Plants: Function and Mechanism

et al. 2021

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Protein persulfidation in plants: mechanisms and functions beyond a simple stress response

Moseler,

Wagner,

Meyer

2024

Biological Chemistry

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Posttranslational modifications (PTMs) can modulate the activity, localization and interactions of proteins and (re)define their biological function. Understanding how changing environments can alter cellular processes thus requires detailed knowledge about the dynamics of PTMs in time and space. A PTM that gained increasing attention in the last decades is protein persulfidation, where a cysteine thiol (-SH) is covalently bound to sulfane sulfur to form a persulfide (-SSH). The precise cellular mechanisms underlying the presumed persulfide signaling in plants are, however, only beginning to emerge. In the mitochondrial matrix, strict regulation of persulfidation and H2S homeostasis is of prime importance for maintaining mitochondrial bioenergetic processes because H2S is a highly potent poison for cytochrome c oxidase. This review summarizes the current knowledge about protein persulfidation and corresponding processes in mitochondria of the model plant Arabidopsis. These processes will be compared to the respective processes in non-plant models to underpin similarities or highlight apparent differences. We provide an overview of mitochondrial pathways that contribute to H2S and protein persulfide generation and mechanisms for H2S fixation and de-persulfidation. Based on current proteomic data, we compile a plant mitochondrial persulfidome and discuss how persulfidation may regulate protein function.

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Interactions of hydrogen sulfide with AhpE from Mycobacterium tuberculosis: formation and reactions of a model peroxiredoxin persulfide

Cited by 2 publications

References 0 publications

Protein Persulfidation in Plants: Function and Mechanism

Protein Persulfidation in Plants: Function and Mechanism

Protein persulfidation in plants: mechanisms and functions beyond a simple stress response

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