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Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii

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Paper breakdownThe authors' claims, conditions and measurements, as JSON Signed receiptProof this review has not been altered
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Christelle Mathé (CEA, LCBM - UMR 5249), Tony A Mattioli (CEA), Olivier Horner (LCBM - UMR 5249), Murielle Lombard (LCBM - UMR 5249), Jean-Marc Latour (LCBM - UMR 5249), Marc Fontecave (LCBM - UMR 5249), Vincent Nivière (LCBM - UMR 5249)

Chemical Physics · Submitted 7 Jan 2015

abstract compiled · 2026-09-23 · no language-model review

The authors' main claim These data support the hypothesis that the reaction of SOR proceeds through such a Fe3+-peroxo intermediate.

how it is stated · hedged possibility 0.80 read the record →

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arXiv ID1501.01470 (version 1)
Pith IDM4CCPDSX, Pith's permanent record of this paper and its review
CitationChristelle Math\'e (CEA, Jean-Marc Latour (LCBM - UMR 5249), LCBM - UMR 5249), Marc Fontecave (LCBM - UMR 5249), Murielle Lombard (LCBM - UMR 5249), Olivier Horner (LCBM - UMR 5249), Tony A Mattioli (CEA), Vincent Nivi\`ere (LCBM - UMR 5249). "Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii." arXiv:1501.01470 (2015). https://pith.science/paper/M4CCPDSX
Claim paper

The compiled record

The paper's own sentences, arranged. Each label is drawn from a closed vocabulary; the number beside it is the probability the classifier gave that label. Numbers in the tables are the authors', checked by code. No sentence in this record was written by a model.

Open the compiled record

Compiled by classifier-1.13-20260917 via OpenRouter, question bank abstract-p1-20260923, 2026-09-23: 1 request, 5,545 input tokens, $0.0002 reported.

What the abstract itself states, as probabilities: claims first 0.04 · states limitation 0.14 · human participants 0.01 · controlled comparison 0.84 · randomized assignment 0.01 · states quantitative result 0.07 · compares with prior results 0.55 · mentions code or data availability 0.02.

The abstract, sentence by sentence

arXiv listing abstract v1. Results and the main claim are underlined; .

The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here, we have reacted the SOR from Desulfoarculus baarsii directly with H2O2. We have found that its active site can transiently stabilize an Fe3+-peroxo species that we have spectroscopically characterized by resonance Raman. The mutation of the strictly conserved Glu47 into alanine results in a stabilization of this Fe3+-peroxo species, when compared to the wild-type form. These data support the hypothesis that the reaction of SOR proceeds through such a Fe3+-peroxo intermediate. This also suggests that Glu47 might serve to help H2O2 release during the reaction with superoxide.

background contribution method result interpretation main claim

What the classifier reports for each sentence. The number is the probability it gave the label.
#sentencerolethe authors' own workstates the main conclusionstrength
s0 The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. background 1.00 0.18 0.03 asserted 1.00
s1 It specifically reduces superoxide to produce H2O2. background 1.00 0.11 0.03 asserted 1.00
s2 Here, we have reacted the SOR from Desulfoarculus baarsii directly with H2O2. method 0.70 0.97 0.02 asserted 1.00
s3 We have found that its active site can transiently stabilize an Fe3+-peroxo species that we have spectroscopically characterized by resonance Raman. result 0.99 0.97 0.28 asserted 1.00
s4 The mutation of the strictly conserved Glu47 into alanine results in a stabilization of this Fe3+-peroxo species, when compared to the wild-type form. result 1.00 0.92 0.09 asserted 1.00
s5 These data support the hypothesis that the reaction of SOR proceeds through such a Fe3+-peroxo intermediate. interpretation 1.00 0.63 0.77 hedged possibility 0.80
s6 This also suggests that Glu47 might serve to help H2O2 release during the reaction with superoxide. interpretation 1.00 0.41 0.11 hedged possibility 0.69

What kind of paper the classifier reports this is: empirical study 1.00 · evidence from observation or experiment 1.00.

What was examined, and what was not

sources read
  • arXiv listing abstract v1
not examined
  • full text
  • figures and tables
  • references and citing sentences
  • relations to other papers
levels run
  • P abstract
not run
  • S sections
  • T body sentences
  • C citations
  • R cross-paper relations

Every quoted sentence on this record is the authors'. Every label is from Pith's closed vocabulary, with the probability shown beside it. Every number in the measurements table is the authors', checked by code. Record as JSON

The paper
Original abstract

The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here, we have reacted the SOR from Desulfoarculus baarsii directly with H2O2. We have found that its active site can transiently stabilize an Fe3+-peroxo species that we have spectroscopically characterized by resonance Raman. The mutation of the strictly conserved Glu47 into alanine results in a stabilization of this Fe3+-peroxo species, when compared to the wild-type form. These data support the hypothesis that the reaction of SOR proceeds through such a Fe3+-peroxo intermediate. This also suggests that Glu47 might serve to help H2O2 release during the reaction with superoxide.

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