Oxalate decarboxylase uses electron hole hopping for catalysis

Pastore, Anthony J.; Teo, Ruijie D.; Montoya, Alvaro; Burg, M.J.; Twahir, Umar T.; Bruner, Steven D.; Beratan, David N.; Angerhofer, Alexander

doi:10.1016/j.jbc.2021.100857

Cited by 8 publications

(21 citation statements)

References 98 publications

(166 reference statements)

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“…The vertical ionization energy (VIE) of the 5‐HTP/W274 pair was calculated following the same procedure as before (Pastore et al, 2021). With only 6.77 eV it was found to be significantly lower than the previously calculated 7.09 eV for the W96/W274 pair in WT enzyme.…”

Section: Resultsmentioning

confidence: 99%

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Selective incorporation of 5‐hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase

et al. 2022

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Oxalate decarboxylase from Bacillus subtilis is a binuclear Mn-dependent acid stress response enzyme that converts the mono-anion of oxalic acid into formate and carbon dioxide in a redox neutral unimolecular disproportionation reaction. A π-stacked tryptophan dimer, W96 and W274, at the interface between two monomer subunits facilitates long-range electron transfer between the two Mn ions and plays an important role in the catalytic mechanism. Substitution of W96 with the unnatural amino acid 5-hydroxytryptophan leads to a persistent EPR signal which can be traced back to the neutral radical of 5-hydroxytryptophan with its hydroxyl proton removed. 5-Hydroxytryptophan acts as a hole sink preventing the formation of Mn(III) at the N-terminal active site and strongly suppresses enzymatic activity. The lower boundary of the standard reduction potential for the active site Mn(II)/Mn(III) couple can therefore be estimated as 740 mV against the normal hydrogen electrode at pH 4, the pH of maximum catalytic efficiency. Our results support the catalytic importance of long-range electron transfer in oxalate decarboxylase while at the same time highlighting the utility of unnatural amino acid incorporation and specifically the use of 5-hydroxytryptophan as an energetic sink for hole hopping to probe electron transfer in redox proteins.

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Section: Resultsmentioning

confidence: 99%

“…This loss of activity is even more pronounced than what we previously observed for the W96F mutation which showed approx. 8% of the catalytic activity of the WT enzyme (Pastore et al, 2021).…”

Section: Enzyme Kineticsmentioning

confidence: 99%

Selective incorporation of 5‐hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase

et al. 2022

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“…The increased level of hydrogen peroxide in the cultures may indicate the oxidative pathway for oxalic acid degradation via oxalate oxidase. The reactive oxygen species were formed in the proposed catalytic cycles of ODC and OXO (Just et al 2004 ; Burrell et al 2007 ; Pastore et al 2021 ). The presence of the hydroperoxyl radical during the turnover of Bacillus subtilis ODC was observed by Twahir et al ( 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Oxalic acid degradation in wood-rotting fungi. Searching for a new source of oxalate oxidase

Grąz

Ruminowicz-Stefaniuk

Jarosz-Wilkołazka

2022

World J Microbiol Biotechnol

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Oxalate oxidase (EC 1.2.3.4) is an oxalate-decomposing enzyme predominantly found in plants but also described in basidiomycete fungi. In this study, we investigated 23 fungi to determine their capability of oxalic acid degradation. After analyzing their secretomes for the products of the oxalic acid-degrading enzyme activity, three groups were distinguished among the fungi studied. The first group comprised nine fungi classified as oxalate oxidase producers, as their secretome pattern revealed an increase in the hydrogen peroxide concentration, no formic acid, and a reduction in the oxalic acid content. The second group of fungi comprised eight fungi described as oxalate decarboxylase producers characterized by an increase in the formic acid level associated with a decrease in the oxalate content in their secretomes. In the secretomes of the third group of six fungi, no increase in formic acid or hydrogen peroxide contents was observed but a decline in the oxalate level was found. The intracellular activity of OXO in the mycelia of Schizophyllum commune, Trametes hirsuta, Gloeophyllum trabeum, Abortiporus biennis, Cerrena unicolor, Ceriosporopsis mediosetigera, Trametes sanguinea, Ceriporiopsis subvermispora, and Laetiporus sulphureus was confirmed by a spectrophotometric assay.

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“…A similar degradative series has been demonstrated in chemical studies using strong oxidants or reductants, with proposed radical intermediates causing decarboxylation and subsequent defluorination (Singh et al ., 2019 ; Su et al ., 2019 ; Filho and Souza, 2020 ; Liu et al ., 2021 ; Palma et al ., 2021 ). Given that radical decarboxylation reactions are well known in biological systems (Liu et al ., 2018 , 2018 , 2018 , 2018 ; Michlits et al ., 2020 ; Rodrigues et al ., 2020 ; Pastore et al ., 2021 ), a radical‐based mechanism for perfluorooctanoate was proposed (Wackett and Robinson, 2020 ). Moreover, radical desulfonation enzymology has been described (Peck et al ., 2019 ; Dawson et al ., 2021 ), and radical desulfonation chemistry for PFAS has been described (Niu et al ., 2016 ).…”

Section: Polyfluorinated Including Perfluorinated Compounds Are Biode...mentioning

confidence: 99%

Nothing lasts forever: understanding microbial biodegradation of polyfluorinated compounds and perfluorinated alkyl substances

Wackett

2021

Microbial Biotechnology

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Poly-and perfluorinated chemicals, including perfluorinated alkyl substances (PFAS), are pervasive in today's society, with a negative impact on human and ecosystem health continually emerging. These chemicals are now subject to strict government regulations, leading to costly environmental remediation efforts. Commercial polyfluorinated compounds have been called 'forever chemicals' due to their strong resistance to biological and chemical degradation. Environmental cleanup by bioremediation is not considered practical currently. Implementation of bioremediation will require uncovering and understanding the rare microbial successes in degrading these compounds. This review discusses the underlying reasons why microbial degradation of heavily fluorinated compounds is rare. Fluorinated and chlorinated compounds are very different with respect to chemistry and microbial physiology. Moreover, the end product of biodegradation, fluoride, is much more toxic than chloride. It is imperative to understand these limitations, and elucidate physiological mechanisms of defluorination, in order to better discover, study, and engineer bacteria that can efficiently degrade polyfluorinated compounds.

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Oxalate decarboxylase uses electron hole hopping for catalysis

Cited by 8 publications

References 98 publications

Selective incorporation of 5‐hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase

Selective incorporation of 5‐hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase

Oxalic acid degradation in wood-rotting fungi. Searching for a new source of oxalate oxidase

Nothing lasts forever: understanding microbial biodegradation of polyfluorinated compounds and perfluorinated alkyl substances

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