The catalytic mechanism of sulfoxide synthases

Stampfli, Anja R.; Seebeck, Florian P.

doi:10.1016/j.cbpa.2020.06.007

Cited by 16 publications

(19 citation statements)

References 46 publications

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“…However, there is ongoing debate regarding the KIE detected and if it is due to the bulky methyl group relative to the hydrogen atom. 149 Although these mechanisms remain to be elucidated, charge maintenance may require attention in their future refinement.…”

Section: Thiol Oxygenasesmentioning

confidence: 99%

Charge Maintenance during Catalysis in Nonheme Iron Oxygenases

Traore

Liu

2022

ACS Catal.

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Here, the choice of the first coordination shell of the metal center is analyzed from the perspective of charge maintenance in a binary enzyme–substrate complex and an O2-bound ternary complex in the nonheme iron oxygenases. Comparing homogentisate 1,2-dioxygenase and gentisate dioxygenase highlights the significance of charge maintenance after substrate binding as an important factor that drives the reaction coordinate. We then extend the charge analysis to several common types of nonheme iron oxygenases containing either a 2-His-1-carboxylate facial triad or a 3-His or 4-His ligand motif, including extradiol and intradiol ring-cleavage dioxygenases, thiol dioxygenases, α-ketoglutarate-dependent oxygenases, and carotenoid cleavage oxygenases. After forming the productive enzyme–substrate complex, the overall charge of the iron complex at the 0, +1, or +2 state is maintained in the remaining catalytic steps. Hence, maintaining a constant charge is crucial to promote the reaction of the iron center beginning from the formation of the Michaelis or ternary complex. The charge compensation to the iron ion is tuned not only by protein-derived carboxylate ligands but also by substrates. Overall, these analyses indicate that charge maintenance at the iron center is significant when all the necessary components form a productive complex. This charge maintenance concept may apply to most oxygen-activating metalloenzymes systems that do not draw electrons and protons step-by-step from a separate reactant, such as NADH, via a reductase. The charge maintenance perception may also be useful in proposing catalytic pathways or designing prototypical reactions using artificial or engineered enzymes for biotechnological applications.

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Section: Thiol Oxygenasesmentioning

confidence: 99%

Charge Maintenance during Catalysis in Nonheme Iron Oxygenases

Traore

Liu

2022

ACS Catal.

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“…The sequences gathered for OvoA and OvoB were first clustered to remove identical entries, and then aligned using MAFFT ( Katoh et al 2019 ) after adding characterized EgtB homologs as outgroup for OvoA-like sequences ( Seebeck 2010 ; Goncharenko et al 2015 ; Stampfli and Seebeck 2020 ) ( Mycolicibacterium smegmatis [WP_011731158.1], Mycolicibacterium thermoresistibile [WP_050811957.1], Mycobacterium tuberculosis [WP_003899647.1], Oscillatoriales cyanobacterium [TAD81928.1], Caenimonas sp. SL110 [WP_048439477.1], Anaeromyxobacter sp.…”

Section: Methodsmentioning

confidence: 99%

Metabolic Adaptations to Marine Environments: Molecular Diversity and Evolution of Ovothiol Biosynthesis in Bacteria

Brancaccio

Tangherlini

Danovaro

et al. 2021

Genome Biology and Evolution

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Ovothiols are sulphur-containing amino acids synthesized by marine invertebrates, protozoans, and bacteria. They act as pleiotropic molecules in signalling and protection against oxidative stress. The discovery of ovothiol biosynthetic enzymes, sulfoxide synthase OvoA and β-lyase OvoB, paves the way for a systematic investigation of ovothiol distribution and molecular diversification in nature. In this work, we conducted genomic and metagenomics data mining to investigate the distribution and diversification of ovothiol biosynthetic enzymes in Bacteria. We identified the bacteria endowed with this secondary metabolic pathway, described their taxonomy, habitat and biotic interactions in order to provide insight into their adaptation to specific environments. We report that OvoA and OvoB are mostly encountered in marine aerobic Proteobacteria, some of them establishing symbiotic or parasitic relationships with other organisms. We identified a horizontal gene transfer event of OvoB from Bacteroidetes living in symbiosis with Hydrozoa. Our search within the Ocean Gene Atlas revealed the occurrence of ovothiol biosynthetic genes in Proteobacteria living in a wide range of pelagic and highly oxygenated environments. Finally, we tracked the evolutionary history of ovothiol biosynthesis from marine bacteria to unicellular eukaryotes and metazoans. Our analysis provides new conceptual elements to unravel the evolutionary and ecological significance of ovothiol biosynthesis.

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“…In a second step, an iron-dependent sulfoxide synthase (EgtB or Egt1, EC 1.14.99.50/52) catalyzes O 2 -dependent coupling of a cysteine or γ-glutamylcysteine to carbon 2 of the imidazole ring of TMH (Figure ). − Subsequent steps trim the resulting sulfoxide intermediate to ergothioneine. A similar pathway emerged by convergent evolution in a small group of cyanobacteria that recruited a sulfoxide synthase from a different process to make ergothioneine .…”

Section: Introductionmentioning

confidence: 99%

Discovery and Characterization of the Metallopterin-Dependent Ergothioneine Synthase from Caldithrix abyssi

Beliaeva

Seebeck

2022

JACS Au

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Ergothioneine is a histidine derivative with a 2-mercaptoimidazole side chain and a trimethylated α-amino group. Although the physiological function of this natural product is not yet understood, the facts that many bacteria, some archaea, and most fungi produce ergothioneine and that plants and animals have specific mechanisms to absorb and distribute ergothioneine in specific tissues suggest a fundamental role in cellular life. The observation that ergothioneine biosynthesis has emerged multiple times in molecular evolution points to the same conclusion. Aerobic bacteria and fungi attach sulfur to the imidazole ring of trimethylhistidine via an O 2 -dependent reaction that is catalyzed by a mononuclear non-heme iron enzyme. Green sulfur bacteria and archaea use a rhodanese-like sulfur transferase to attach sulfur via oxidative polar substitution. In this report, we describe a third unrelated class of enzymes that catalyze sulfur transfer in ergothioneine production. The metallopterin-dependent ergothioneine synthase from Caldithrix abyssi contains an N-terminal module that is related to the tungsten-dependent acetylene hydratase and a C-terminal domain that is a functional cysteine desulfurase. The two modules cooperate to transfer sulfur from cysteine onto trimethylhistidine. Inactivation of the C-terminal desulfurase blocks ergothioneine production but maintains the ability of the metallopterin to exchange sulfur between ergothioneine and trimethylhistidine. Homologous bifunctional enzymes are encoded exclusively in anaerobic bacterial and archaeal species.

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The catalytic mechanism of sulfoxide synthases

Cited by 16 publications

References 46 publications

Charge Maintenance during Catalysis in Nonheme Iron Oxygenases

Charge Maintenance during Catalysis in Nonheme Iron Oxygenases

Metabolic Adaptations to Marine Environments: Molecular Diversity and Evolution of Ovothiol Biosynthesis in Bacteria

Discovery and Characterization of the Metallopterin-Dependent Ergothioneine Synthase from Caldithrix abyssi

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