Hydrogen peroxide-independent generation of superoxide catalyzed by soybean peroxidase in response to ferrous ion

Kimura, Makoto; Kawano, Tomonori

doi:10.1080/15592324.2015.1010917

Cited by 3 publications

(4 citation statements)

References 27 publications

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“…Halliwell (1978) also demonstrated that peroxidase-catalyzed H 2 O 2 /O 2 − generation largely depends on both Mn 2+ and phenolic compounds such as p-CA. In fact, exclusion of either NADH, Mn 2+ or p-CA significantly lowered the O 2 − -generating activity in extracts from Arabidopsis cell walls (data not shown), confirming that cell wall peroxidase(s) itself is capable of generating ROS through the oxygen-requiring cycle independently of H 2 O 2 as reported previously (Kimura and Kawano 2015). Collectively, PRX34 is likely one of the important isoforms that generate ROS through the oxidation of NADH.…”

Section: Introductionsupporting

confidence: 84%

“…Apoplastic class III peroxidases (EC 1.11.1.7) comprise a large protein family thought to be involved in diverse functions in plants due to their catalytic versatility and numerous isoforms (Shigeto and Tsutsumi 2016;Tognolli et al 2002;Welinder et al 2002). Peroxidases usually catalyze the oxidation of substrates via hydrogen peroxide (H 2 O 2 ), whereas some isoforms of this family can generate reactive oxygen species (ROS) at a neutral to basic pH in the presence of some reductants (Bolwell et al 1998(Bolwell et al , 2002Kawano 2003; Kimura and Kawano 2015;O'Brien et al 2012a). To date, the apoplastic peroxidase-dependent oxidative burst in response to an elicitor or microbe-associated molecular pattern (MAMP) has been validated in French bean (Bolwell et al 1998), Arabidopsis (Bindschedler et al 2006;Davies et al 2006;O'Brien et al 2012b), pepper (Choi et al 2007), lettuce (Bestwick et al 1998) and pea (Kiba et al 1997).…”

Section: Introductionmentioning

confidence: 99%

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A class III peroxidase PRX34 is a component of disease resistance in Arabidopsis

et al. 2019

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PRX34 mediates the oxidative burst in Arabidopsis. Here we characterized two additional Arabidopsis prx34 null mutants (prx34-2, prx34-3), besides the well-studied prx34-1. Due to a decrease in corresponding peroxidase, the activity that generates reactive oxygen species (ROS) was significantly lower in cell wall extracts of prx34-2 and prx34-3 plants. Consistently, the prx34-2 and prx34-3 exhibited reduced accumulation both of ROS and callose in Flg22-elicitor-treated leaves, leading to enhanced susceptibility to bacterial and fungal pathogens. In contrast, ectopic expression of PRX34 in the wild type caused enhanced resistance. PRX34 is thus a component for disease resistance in Arabidopsis.

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Section: Introductionsupporting

confidence: 84%

Section: Introductionmentioning

confidence: 99%

A class III peroxidase PRX34 is a component of disease resistance in Arabidopsis

et al. 2019

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“…Formation of compound I by Hcy treatment in absence of H 2 O 2 means that the oxidase cycle is followed by peroxidase cycle. Interestingly, production of O 2 ˙ ® anions under oxidase cycle has been reported on some HRP variants in presence of salicylic acid or indole 3 acetic acid as substrates [ 43 , 44 ]. According to oxidase cycle, using molecular O 2 , the ferrous iron (Fe 2+ ) is converted to unstable compound III (Fe 3+ ) form thereby forming O 2 -Heme-Fe 2+ or O 2 ˙̅ -Heme-Fe 3+ .…”

Section: Discussionmentioning

confidence: 99%

Functional inhibition of redox regulated heme proteins: A novel mechanism towards oxidative stress induced by homocysteine

2021

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Homocysteine (Hcy) is a sulfur containing non-protein toxic amino acid synthesized from methionine. Elevated level of Hcy is associated with cardiovascular complications and neurodegeneration. Hcy is believed to induce organ damage and apoptosis via oxidative stress. The pro-oxidant nature of Hcy is considered to originate from the metal-induced oxidation of thiol group-containing molecules forming disulfides (Hcy-Hcy, Hcy-cysteine, Hcy-glutathione, etc) or with free cysteine residues of proteins (a process called protein S-homocysteinylation). Formation of such disulfides indeed results in the generation of reactive oxygen species (ROS) which eventually leads to loss of cellular integrity. In the present manuscript, we performed systematic investigation of the effect of Hcy on iron containing proteins. We discover a novel mechanism of Hcy toxicity wherein Hcy oxidation is linked with the functional loss of the protein with iron as cofactors. Our results indicate that redox regulated heme proteins might be primarily involved in the Hcy toxicity and associated oxidative stress.

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“…Furthermore, APEX tends to favor labeling of unfolded proteins (Minde et al, 2018), so there is certainly the possibility for biased outcomes. Soybean peroxidase is known to generate spontaneous reactive oxygen species under certain conditions, and hence APEX could confer context specific changes to cellular redox levels that are difficult to address (Kimura and Kawano, 2015). How the ectopic overexpression of peroxidase may alter signaling/interactome architectures and redox homeostasis, etc., has not yet been assessed.…”

Section: Parametersmentioning

confidence: 99%

Chemical Biology Gateways to Mapping Location, Association, and Pathway Responsivity

2019

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Here we discuss, how by applying chemical concepts to biological problems, methods have been developed to map spatiotemporal regulation of proteins and small-molecule modulation of proteome signaling responses. We outline why chemical-biology platforms are ideal for such purposes. We further discuss strengths and weaknesses of chemical-biology protocols, contrasting them against classical genetic and biochemical approaches. We make these evaluations based on three parameters: occupancy; functional information; and spatial restriction. We demonstrate how the specific choice of chemical reagent and experimental set-up unite to resolve biological problems. Potential improvements/extensions as well as specific controls that in our opinion are often overlooked or employed incorrectly are also considered. Finally, we discuss some of the latest emerging methods to illuminate how chemical-biology innovations provide a gateway toward information hitherto inaccessible by conventional genetic/biochemical means. Finally, we also caution against solely relying on chemical-biology strategies and urge the field to undertake orthogonal validations to ensure robustness of results.

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Hydrogen peroxide-independent generation of superoxide catalyzed by soybean peroxidase in response to ferrous ion

Cited by 3 publications

References 27 publications

A class III peroxidase PRX34 is a component of disease resistance in Arabidopsis

A class III peroxidase PRX34 is a component of disease resistance in Arabidopsis

Functional inhibition of redox regulated heme proteins: A novel mechanism towards oxidative stress induced by homocysteine

Chemical Biology Gateways to Mapping Location, Association, and Pathway Responsivity

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