Isotope-labeled ergothioneine clarifies the mechanism of reaction with singlet oxygen

Hartmann, Lea; Seebeck, Florian P.; Schmalz, Hans‐Günther; Gründemann, Dirk

doi:10.1016/j.freeradbiomed.2023.01.023

Cited by 7 publications

(3 citation statements)

References 31 publications

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“…In addition, these authors suggest that this process could occur inside cells, not just in vitro, as when exposing endothelial cells to oxidative stress caused by high glucose levels, paraquat, superoxide, or hydrogen peroxide [ 45 ], although the reaction kinetics may not favor this process in vivo. Nonetheless, there is not universal agreement regarding this proposed mechanism [ 46 ]. For example, an alternate proposal suggests that when ESH is oxidized by, for example, the hydroxyl radical, it can be “repaired” (i.e., regenerated) by interacting with vitamin C, which reduces oxidized ESH and simultaneously generates the ascorbyl radical [ 47 ]; of course, in cells, the ascorbyl radical would then need to be reduced [ 48 ].…”

Section: Esh Mechanism(s) Of Action: What Does It Do and How Does It ...mentioning

confidence: 99%

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The Role of Ergothioneine in Red Blood Cell Biology: A Review and Perspective

Thomas,

Francis,

Zimring

et al. 2024

Antioxidants

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Oxidative stress can damage tissues and cells, and their resilience or susceptibility depends on the robustness of their antioxidant mechanisms. The latter include small molecules, proteins, and enzymes, which are linked together in metabolic pathways. Red blood cells are particularly susceptible to oxidative stress due to their large number of hemoglobin molecules, which can undergo auto-oxidation. This yields reactive oxygen species that participate in Fenton chemistry, ultimately damaging their membranes and cytosolic constituents. Fortunately, red blood cells contain robust antioxidant systems to enable them to circulate and perform their physiological functions, particularly delivering oxygen and removing carbon dioxide. Nonetheless, if red blood cells have insufficient antioxidant reserves (e.g., due to genetics, diet, disease, or toxin exposure), this can induce hemolysis in vivo or enhance susceptibility to a “storage lesion” in vitro, when blood donations are refrigerator-stored for transfusion purposes. Ergothioneine, a small molecule not synthesized by mammals, is obtained only through the diet. It is absorbed from the gut and enters cells using a highly specific transporter (i.e., SLC22A4). Certain cells and tissues, particularly red blood cells, contain high ergothioneine levels. Although no deficiency-related disease has been identified, evidence suggests ergothioneine may be a beneficial “nutraceutical.” Given the requirements of red blood cells to resist oxidative stress and their high ergothioneine content, this review discusses ergothioneine’s potential importance in protecting these cells and identifies knowledge gaps regarding its relevance in enhancing red blood cell circulatory, storage, and transfusion quality.

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Section: Esh Mechanism(s) Of Action: What Does It Do and How Does It ...mentioning

confidence: 99%

“…[ 44 ]). Nonetheless, other pathways have been proposed, including ones involving GSH to regenerate reduced ESH [ 46 , 47 , 49 , 51 ].…”

Section: Figurementioning

confidence: 99%

The Role of Ergothioneine in Red Blood Cell Biology: A Review and Perspective

Thomas,

Francis,

Zimring

et al. 2024

Antioxidants

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“…Over recent years, growing evidence has indicated a link between Ergothioneine and GSH function. Ergothioneine eliminates ROS through direct or indirect mechanisms thereby modulating the cellular GSH redox state ( Jacob, 2006 ; Servillo et al, 2015 ; Oumari et al, 2019 ; Hartmann et al, 2023 ). Second, GSH redox status influences the activity of SAM synthase (also named methionine adenosyl-transferase), in which a high [GSH]/[GSSG] (glutathione disulfide) ratio promotes SAM synthase to achieve its maximum activity ( Pajares et al, 1992 ; Rahman et al, 2003 ; Hitchler and Domann, 2007 ).…”

Section: Ergothioneine and Its Proposed Anti-ageing Mechanismsmentioning

confidence: 99%

Ergothioneine and its congeners: anti-ageing mechanisms and pharmacophore biosynthesis

Chen

Zhang

et al. 2023

Protein &Amp; Cell

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Ergothioneine, Ovothiol and Selenoneine are sulfur/selenium-containing histidine-derived natural products widely distributed across different organisms. They exhibit significant antioxidant properties, making them as potential lead compounds for promoting health. Increasing evidence suggests that Ergothioneine is positively correlated with healthy ageing and longevity. The mechanisms underlying Ergothioneine regulation of the ageing process at cellular and molecular level are beginning to be understood. In this review, we provide an in-depth and extensive coverage of the anti-ageing studies on Ergothioneine and discuss its possible intracellular targeting pathways. In addition, we highlight the recent efforts in elucidating the biosynthetic details for Ergothioneine, Ovothiol and Selenoneine, with a particular focus on the study of their pharmacophore-forming enzymology.

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Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

Nalivaiko,

Vasseur,

Seebeck

2024

Angewandte Chemie

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Ergothioneine is a sulfur‐containing metabolite that is produced by bacteria and fungi, and is absorbed by plants and animals as a micronutrient. Ergothioneine reacts with harmful oxidants including singlet oxygen or hydrogen peroxide, and may therefore protect cells against oxidative stress. In this report we describe two enzymes from actinobacteria that cooperate in the specific oxidative degradation of ergothioneine. The first enzyme is an iron‐dependent thiol dioxygenase that produces ergothioneine sulfinic acid. A crystal structure of ergothioneine dioxygenase from Thermocatellispora tengchongensis reveals many similarities with cysteine dioxygenases, suggesting that the two enzymes share a common mechanism. The second enzyme is a metal‐dependent ergothioneine sulfinic acid desulfinase that produces Na‐trimethylhistidine and SO2. The discovery that certain actinobacteria contain the enzymatic machinery for O2‐dependent biosynthesis and O2‐dependent degradation of ergothioneine indicates that these organisms may actively manage their ergothioneine content

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Isotope-labeled ergothioneine clarifies the mechanism of reaction with singlet oxygen

Cited by 7 publications

References 31 publications

The Role of Ergothioneine in Red Blood Cell Biology: A Review and Perspective

The Role of Ergothioneine in Red Blood Cell Biology: A Review and Perspective

Ergothioneine and its congeners: anti-ageing mechanisms and pharmacophore biosynthesis

Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine

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