Ab initio studies of the properties of intracellular thiols ergothioneine and ovothiol

Hand, Christine E.; Taylor, Nicholas J.; Honek, John F.

doi:10.1016/j.bmcl.2005.01.014

Cited by 28 publications

(31 citation statements)

References 42 publications

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“…The calculated C2-N1 and C2-N3 bonds are 1.375 Å and 1.367 Å which are little larger than the experimental ones with amount of 0.025 Å and 0.017 Å [4]. The C4=C5 bond of 1.357 Å is quite close to the XRD data (1.350 Å) [5]. Based on this analysis, the B3LYP/6-311G(d,p) method can be considered as the good method to provide the suitable structures for the next calcualtions.…”

Section: Stable Conformation Of Eshsupporting

confidence: 62%

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Thermochemical Parameters of Ergothioneine: A DFT Study Using M06, Wb97xd and TPSSTPSS Methods

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2018

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Antioxidant properties of ergothioneine (ESH) have been investigated via hydrogen atom transfer (HAT), single electron transfer-proton transfer (SET-PT) and sequential proton loss electron transfer (SPLET) mechanisms. Three new DFT methods including M06, WB97XD and TPSSTPSS at the 6-311++G(2df,2p) basis set were used to compute the thermochemical parameters of ESH in the gas phase. Based on these methods, bond dissociation enthalpy (BDE), ionization energy (IE), proton dissociation enthalpy (PDE), proton affinity (PA) and electron transfer enthalpy (ETE) were calculated. The results were also compared with the values obtained by B3LYP method. The calculated results show that ergothioneine plays a role as a potential antioxidant via HAT mechanism.

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Section: Stable Conformation Of Eshsupporting

confidence: 62%

“…In comparison with the x-ray diffraction (XRD) data [5], the B3LYP/6-311G(d,p) geometrical parameters of ESH A slightly deviate from the experimental values. For example, the calculated and experimental data of the C=S bonds are 1.678 Å and 1.690 Å, respectively.…”

Section: Stable Conformation Of Eshmentioning

confidence: 99%

Thermochemical Parameters of Ergothioneine: A DFT Study Using M06, Wb97xd and TPSSTPSS Methods

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2018

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“…The free energy of reduction of ergothioneine disulfide (ESSE), lower than those of alkyldisulfides, has been ascribed to the thermodynamic stability of the thione form [20]. Actually, in the totality of the proposed mechanisms of its antioxidant function, ESH is considered to oscillate between the reduced state and the oxidized state represented by the disulfide form, similarly to alkylthiols such as cysteine or glutathione [19,26].…”

Section: Introductionmentioning

confidence: 99%

An uncommon redox behavior sheds light on the cellular antioxidant properties of ergothioneine

Servillo

Castaldo

Casale

et al. 2015

Free Radical Biology and Medicine

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“…In M. smegmatis, ESH biosynthesis is initiated by a methyltransferase (EgtD), and proceeds through an additional five-step pathway involving the enzymes EgtA-E [4]. Unlike other LMW thiols such as MSH, ESH is tautomeric [5] and exists predominantly in the thione form in neutral aqueous solutions. In addition, the redox potential of ESH is −60mV as compared to −250 mV of GSH which may account for ESH’s resistance to auto-oxidation [5].…”

Section: Introductionmentioning

confidence: 99%

“…Unlike other LMW thiols such as MSH, ESH is tautomeric [5] and exists predominantly in the thione form in neutral aqueous solutions. In addition, the redox potential of ESH is −60mV as compared to −250 mV of GSH which may account for ESH’s resistance to auto-oxidation [5]. …”

Section: Introductionmentioning

confidence: 99%

Lack of mycothiol and ergothioneine induces different protective mechanisms in Mycobacterium smegmatis

Singh

Strankman

Orkusyan

et al. 2016

Biochemistry and Biophysics Reports

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Mycobacterium smegmatis contains the low molecular weight thiols, mycothiol (MSH) and ergothioneine (ESH). Examination of transposon mutants disrupted in mshC and egtA, involved in the biosynthesis of MSH and ESH respectively, demonstrated that both mutants were sensitive to oxidative, alkylating, and metal stress. However, the mshC mutant exhibited significantly more protein carbonylation and lipid peroxidation than wildtype, while the egtA mutant had less protein and lipid damage than wildtype. We further show that Ohr, KatN, and AhpC, involved in protection against oxidative stress, are upregulated in the egtA mutant. In the mshC mutant, an Usp and a putative thiol peroxidase are upregulated. In addition, mutants lacking MSH also contained higher levels of Coenzyme F420 as compared to wildtype and two Coenzyme F420 dependent enzymes were found to be upregulated. These results indicate that lack of MSH and ESH result in induction of different mechanisms for protecting against oxidative stress.

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Ab initio studies of the properties of intracellular thiols ergothioneine and ovothiol

Cited by 28 publications

References 42 publications

Thermochemical Parameters of Ergothioneine: A DFT Study Using M06, Wb97xd and TPSSTPSS Methods

Thermochemical Parameters of Ergothioneine: A DFT Study Using M06, Wb97xd and TPSSTPSS Methods

An uncommon redox behavior sheds light on the cellular antioxidant properties of ergothioneine

Lack of mycothiol and ergothioneine induces different protective mechanisms in Mycobacterium smegmatis

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