Evidence map›Paper›PMID 38505375›Full record

ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2021

XFEL Crystal Structures of Peroxidase Compound II.

Hanna Kwon, Jaswir Basran, Chinar Pathak, Mahdi Hussain, Samuel L Freeman, Alistair J Fielding, Anna J Bailey, Natalia Stefanou, Hazel A Sparkes, Takehiko Tosha and 12 more

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. XFEL Crystal Structures of Peroxidase Compound II.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
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

22 authors at 7 institutions in 2 countries.

Hanna KwonSchool of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID 0000-0001-6941-4808
Jaswir BasranDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology University of Leicester Lancaster Road Leicester LE1 7RH UK.ORCID 0000-0003-2273-7348
Chinar PathakDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology University of Leicester Lancaster Road Leicester LE1 7RH UK.
Mahdi HussainDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology University of Leicester Lancaster Road Leicester LE1 7RH UK.
Samuel L FreemanSchool of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.
Alistair J FieldingCentre for Natural Products Discovery, Pharmacy and Biomolecular Sciences Liverpool John Moores University James Parsons Building, Byrom Street Liverpool L3 3AF UK.
Anna J BaileySchool of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.
Natalia StefanouSchool of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.
Hazel A SparkesSchool of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.
Takehiko ToshaRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Keitaro YamashitaRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Kunio HirataRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Hironori MurakamiJapan Synchrotron Radiation Research Institute 1-1-1 Kouto Sayo Hyogo 679-5198 Japan.
Go UenoRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Hideo AgoRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Kensuke TonoJapan Synchrotron Radiation Research Institute 1-1-1 Kouto Sayo Hyogo 679-5198 Japan.
Masaki YamamotoRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Hitomi SawaiGraduate School of Life Science University of Hyogo 3-2-1 Kouto, Kamigori-cho Ako-gun Hyogo 678-1297 Japan.
Yoshitsugu ShiroGraduate School of Life Science University of Hyogo 3-2-1 Kouto, Kamigori-cho Ako-gun Hyogo 678-1297 Japan.
Hiroshi SugimotoRIKEN SPring-8 Center 1-1-1 Kouto Sayo Hyogo 679-5148 Japan.
Emma L RavenSchool of Chemistry University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID 0000-0002-1643-8694
Peter C E MoodyDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology University of Leicester Lancaster Road Leicester LE1 7RH UK.ORCID 0000-0003-1762-9238
SPring-8 · JPUniversity of Bristol · GBUniversity of Leicester · GBJapan Synchrotron Radiation Research Institute · JPUniversity of Hyogo · JPLiverpool John Moores University · GBMRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxygen activation in all heme enzymes requires the formation of high oxidation states of iron, usually referred to as ferryl heme. There are two known intermediates: Compound I and Compound II. The nature of the ferryl heme-and whether it is an Fe

Indexed as

hemeheme proteinsperoxidase

Identifiers

PMID38505375
PMCPMC10947387
OpenAlexW4249177945

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.