Deactivation of Hemeperoxidases by Hydrogen Peroxide: Focus on Compound III

Valderrama, Brenda

doi:10.1007/978-3-642-12627-7_11

Cited by 14 publications

(24 citation statements)

References 141 publications

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“…The spectrum measured in the presence of hydrogen peroxide shows a significant decrease in the Soret band intensity and disappearance of the Q bands at 503 nm and 630 nm that is unlike the characteristic spectrum of HRP-Compound III. However, the formation of Compound III may be transient for Orf13 even though this heme-iron state has been shown to be stable in HRP for at least five minutes (56). This may suggest a different hydrogen peroxide inactivation mechanism for Orf13.…”

Section: Resultsmentioning

confidence: 99%

“…40 Characteristic bands for compound III in HRP include a Soret band at 417 nm and Q-bands at 544 and 580 nm. 56 For Orf13, reversed substrate order of addition is necessary for catalysis with preincubation with L-tyrosine prior to the addition of hydrogen peroxide (Figure S10). No turnover is observed if hydrogen peroxide is incubated with Orf13 before the addition of Ltyrosine.…”

Section: Biochemistrymentioning

confidence: 99%

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A Heme Peroxidase with a Functional Role as an l-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin

2011

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We report the first characterization and classification of Orf13 (S. refuineus) as a heme dependent peroxidase catalyzing the ortho-hydroxylation of l-tyrosine to l-DOPA. The putative tyrosine hydroxylase coded by orf13 of the anthramycin biosynthesis gene cluster has been expressed and purified. Heme b has been identified as the required cofactor for catalysis and maximal l-tyrosine conversion to l-DOPA is observed in the presence of hydrogen peroxide. Pre-incubation of l-tyrosine with Orf13 prior to the addition of hydrogen peroxide is required for l-DOPA production. However, the enzyme becomes inactivated by hydrogen peroxide during catalysis. Steady state kinetic analysis of l-tyrosine hydroxylation revealed similar catalytic efficiency for both l-tyrosine and hydrogen peroxide. Spectroscopic data from a reduced-CO (g) UV-visible spectrum of Orf13 and electron paramagnetic resonance of ferric-heme Orf13 are consistent with heme peroxidases that have a histidyl-ligated heme-iron. Contrary to the classical heme peroxidase oxidation reaction with hydrogen peroxide that produces coupled aromatic products such as o,o'-dityrosine, Orf13 is novel in its ability to catalyze aromatic amino acid hydroxylation with hydrogen peroxide, in the substrate addition order and for its substrate specificity for l-tyrosine. Peroxygenase activity of Orf13 for the ortho-hydroxylation of l-tyrosine to l-DOPA by a molecular oxygen dependent pathway in the presence of dihydroxyfumaric acid is also observed. This reaction behavior is consistent with peroxygenase activity reported with horseradish peroxidase for the hydroxylation of phenol. Overall, the putative function of Orf13 as a tyrosine hydroxylase has been confirmed and establishes the first bacterial class of tyrosine hydroxylases.

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Section: Resultsmentioning

confidence: 99%

Section: Biochemistrymentioning

confidence: 99%

A Heme Peroxidase with a Functional Role as an l-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin

2011

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“…Although H 2 O 2 is distributed in almost all organisms, when its concentration exceeds a certain threshold, it could cause adverse effects, such as cytotoxicity and enzyme inhibition ( Valderrama, 2010 ). A high concentration of H 2 O 2 would affect cell growth and limited the production of target products ( Niu et al, 2014 ; Cheng et al, 2021b ).…”

Section: Resultsmentioning

confidence: 99%

An Artificial Pathway for N-Hydroxy-Pipecolic Acid Production From L-Lysine in Escherichia coli

Luo

Wang

et al. 2022

Front. Microbiol.

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N-hydroxy-pipecolic acid (NHP) is a hydroxylated product of pipecolic acid and an important systemic acquired resistance signal molecule. However, the biosynthesis of NHP does not have a natural metabolic pathway in microorganisms. Here, we designed and constructed a promising artificial pathway in Escherichia coli for the first time to produce NHP from biomass-derived lysine. This biosynthesis route expands the lysine catabolism pathway and employs six enzymes to sequentially convert lysine into NHP. This artificial route involves six functional enzyme coexpression: lysine α-oxidase from Scomber japonicus (RaiP), glucose dehydrogenase from Bacillus subtilis (GDH), Δ1-piperideine-2-carboxylase reductase from Pseudomonas putida (DpkA), lysine permease from E. coli (LysP), flavin-dependent monooxygenase (FMO1), and catalase from E. coli (KatE). Moreover, different FMO1s are used to evaluate the performance of the produce NHP. A titer of 111.06 mg/L of NHP was yielded in shake flasks with minimal medium containing 4 g/L of lysine. By this approach, NHP has so far been produced at final titers reaching 326.42 mg/L by 48 h in a 5-L bioreactor. To the best of our knowledge, this is the first NHP process using E. coli and the first process to directly synthesize NHP by microorganisms. This study lays the foundation for the development and utilization of renewable resources to produce NHP in microorganisms.

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“…The resulting compound II can further react in a second one electron oxidation reaction with the substrate or react with another H 2 O 2 molecule. 53 The latter reaction leads to the formation of compound III. This compound III can be described as peroxy-Fe III porphyrin free radical.…”

Section: Peroxidase Treatment Of Final Effluent and D 0 Filtratementioning

confidence: 99%

“…This compound III can be described as peroxy-Fe III porphyrin free radical. 53 The hypothesized heme auto hydroxylation forms α-meso-hydroxyheme. 54,55 Rearrangement to verdoheme and lastly biliverdin formation leads to heme bleaching and loss of enzyme activity.…”

Section: Peroxidase Treatment Of Final Effluent and D 0 Filtratementioning

confidence: 99%

Removal of hard COD from acidic eucalyptus kraft pulp bleach plant effluent streams using oxidoreductases

Herold-Majumdar

Pita

Estevez

et al. 2021

Biotech and App Biochem

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The bleach plant of a pulp and paper (P&P) mill presents a major source of wastewater containing toxic organic matter characterized as chemical oxygen demand (COD). Due to their high oxidizing power, oxidoreductases hold promise to be a key solution for the removal of dissolved organic material. Here, four oxidoreductases from different enzyme families were selected to treat bleach plant effluents. Haloperoxidase treatment of the final effluent resulted in the highest levels of decolorization (71%) and reduction of aromatic compounds (36%). Using single compound analysis, 27 low molecular weight compounds were found to be persistent throughout the wastewater treatment process and, therefore, classified as hard COD. The tested enzymes efficiently removed several of the identified COD compounds. Hence, this study suggests that the application of oxidoreductases will serve as an environmental-friendly solution for reducing waste from P&P production.

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Deactivation of Hemeperoxidases by Hydrogen Peroxide: Focus on Compound III

Cited by 14 publications

References 141 publications

A Heme Peroxidase with a Functional Role as an l-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin

A Heme Peroxidase with a Functional Role as an l-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin

An Artificial Pathway for N-Hydroxy-Pipecolic Acid Production From L-Lysine in Escherichia coli

Removal of hard COD from acidic eucalyptus kraft pulp bleach plant effluent streams using oxidoreductases

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