Evidence map›Paper›PMID 36366763›Full record

ArticleACS catalysis2022

Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound I in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB.

Marina Lučić, Michael T Wilson, Takehiko Tosha, Hiroshi Sugimoto, Anastasya Shilova, Danny Axford, Robin L Owen, Michael A Hough, Jonathan A R Worrall

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 15 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Marina LučićSchool of Life Sciences, University of Essex, Wivenhoe Park, Essex, ColchesterCO4 3SQ, U.K.
Michael T WilsonSchool of Life Sciences, University of Essex, Wivenhoe Park, Essex, ColchesterCO4 3SQ, U.K.
Takehiko ToshaRIKEN, Spring-8 Center, 1-1-1 Kouto, Sayo, Hyogo679-5148Japan.ORCID https://orcid.org/0000-0002-8971-0759
Hiroshi SugimotoRIKEN, Spring-8 Center, 1-1-1 Kouto, Sayo, Hyogo679-5148Japan.ORCID https://orcid.org/0000-0002-3140-8362
Anastasya ShilovaDiamond Light Source, Harwell Science and Innovation Campus, Oxfordshire, DidcotOX11 0DE, U.K.
Danny AxfordDiamond Light Source, Harwell Science and Innovation Campus, Oxfordshire, DidcotOX11 0DE, U.K.
Robin L OwenDiamond Light Source, Harwell Science and Innovation Campus, Oxfordshire, DidcotOX11 0DE, U.K.
Michael A HoughSchool of Life Sciences, University of Essex, Wivenhoe Park, Essex, ColchesterCO4 3SQ, U.K.
Jonathan A R WorrallSchool of Life Sciences, University of Essex, Wivenhoe Park, Essex, ColchesterCO4 3SQ, U.K.ORCID https://orcid.org/0000-0002-1863-834X
University of Essex · GBDiamond Light Source · GBSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Controlling the reactivity of high-valent Fe(IV)-O catalytic intermediates, Compounds I and II, generated in heme enzymes upon reaction with dioxygen or hydrogen peroxide, is important for function. It has been hypothesized that the presence (wet) or absence (dry) of distal heme pocket water molecules can influence whether Compound I undergoes sequential one-electron additions or a concerted two-electron reduction. To test this hypothesis, we investigate the role of water in the heme distal pocket of a dye-decolorizing peroxidase utilizing a combination of serial femtosecond crystallography and rapid kinetic studies. In a dry distal heme site, Compound I reduction proceeds through a mechanism in which Compound II concentration is low. This reaction shows a strong deuterium isotope effect, indicating that reduction is coupled to proton uptake. The resulting protonated Compound II (Fe(IV)-OH) rapidly reduces to the ferric state, giving the appearance of a two-electron transfer process. In a wet site, reduction of Compound I is faster, has no deuterium effect, and yields highly populated Compound II, which is subsequently reduced to the ferric form. This work provides a definitive experimental test of the hypothesis advanced in the literature that relates sequential or concerted electron transfer to Compound I in wet or dry distal heme sites.

Identifiers

PMID36366763
PMCPMC9638988
OpenAlexW4306699933

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.