Evidence map›Paper›PMID 40009202›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2025

Cytochromes P460 and c'-β: exploiting a novel fold for multiple functions.

Hannah R Adams, Sotaro Fujii, Hans E Pfalzgraf, Peter Smyth, Colin R Andrew, Michael A Hough

Abstract readReview
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2025. 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
–field-weighted citation impact
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.

  1. 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

6 authors.

Hannah R AdamsSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK. hradam@essex.ac.uk.
Sotaro FujiiGraduate School of Biosphere Science, Hiroshima University, Kagamiyama 1-4-4, Higashi-Hiroshima, Hiroshima, 739-8528, Japan.
Hans E PfalzgrafDiamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK.
Peter SmythSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK.
Colin R AndrewDepartment of Chemistry & Biochemistry, Eastern Oregon University, La Grande, OR, 97850, USA. candrew@eou.edu.
Michael A HoughSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK. Michael.Hough@Diamond.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/V01577X/1National Science Foundation MCB-1411963
6 · The paper itself

Abstract

Two related classes of ligand-binding heme c-containing proteins with a high degree of structural homology have been identified and characterized over recent decades: cytochromes P460 (cyts P460), defined by an unusual heme-lysine cross-link, and cytochromes c'-β (cyts c'-β), containing a canonical c-heme without the lysine cross-link. The shared protein fold of the cyt P460-cyt c'-β superfamily can accommodate a variety of heme environments with entirely different reactivities. On the one hand, cyts P460 with polar distal pockets have been shown to oxidize NH

Indexed as

Cytochromes c'HemeHumansModels, MolecularProtein FoldingCytochromes c'HemeCross-linkGas bindingHaemHemeNitrificationP460

Identifiers

PMID40009202
PMCPMC11928373

What OpenQuestion holds

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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.