Evidence map›Paper›PMID 40450052›Full record

ArticleApplied microbiology and biotechnology2025

Characterisation of the thermophilic P450 CYP116B305 identified using metagenomics-derived sequence data from an Australian hot spring.

Simran Kundral, Peter D Giang, Leah R Grundon, Jenna M Supper, Sunil K Khare, Paul V Bernhardt, Paul Evans, Stephen G Bell, James J De Voss

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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.

Simran KundralThe University of Queensland, Australia - Indian Institute of Technology Delhi Research Academy (UQIDRA), Delhi, India.ORCID http://orcid.org/0000-0002-4225-9016
Peter D GiangSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.ORCID http://orcid.org/0000-0002-1408-997X
Leah R GrundonAustralian Centre for Ecogenomics, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, 4072, Australia.
Jenna M SupperAustralian Centre for Ecogenomics, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, 4072, Australia.ORCID http://orcid.org/0009-0006-7129-2276
Sunil K KhareEnzyme and Microbial Biochemistry Laboratory, Department of Chemistry, Indian Institute of Technology Delhi, New Delhi, India.ORCID http://orcid.org/0000-0002-7339-3058
Paul V BernhardtSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.ORCID http://orcid.org/0000-0001-6839-1763
Paul EvansAustralian Centre for Ecogenomics, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, 4072, Australia.
Stephen G BellDepartment of Chemistry, The University of Adelaide, Adelaide, SA, 5005, Australia.ORCID http://orcid.org/0000-0002-7457-9727
James J De VossSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia. j.devoss@uq.edu.au.ORCID http://orcid.org/0000-0002-2659-5140

Funding

Australian Research Council DP240101500Australian Research Council FT210100812
6 · The paper itself

Abstract

Cytochrome P450 enzymes (P450s) have gained significant attention due to their remarkable ability to oxidise unactivated C-H bonds with high regio- and stereoselectivity. Their industrial utility is often limited by challenges such as low stability, poor expression, and dependence on elusive redox partners. These issues have driven the search for more robust P450s, especially those that are inherently stable under extreme conditions typical of industrial processes. "Self-sufficient P450s" in which the P450 heme domain is naturally fused to redox domains in a single polypeptide chain eliminates the need to identify and separately express required redox partners. Furthermore, P450s from thermophilic organisms are more temperature tolerant with fewer stability issues. This study presents a self-sufficient P450, CYP116B305, identified from metagenomically assembled genomes from Innot Hot Springs (71 °C), located in North Queensland, Australia. CYP116B305 was heterologously expressed in Escherichia coli and purified using standard protocols. Investigation of the thermal stability of CYP116B305 revealed a robust heme domain with a

Indexed as

Cytochrome P-450 Enzyme SystemHot SpringsAustraliaEnzyme StabilityEscherichia coliHemeHot TemperatureMetagenomicsOxidation-ReductionQueenslandRecombinant ProteinsCytochrome P-450 Enzyme SystemHemeRecombinant ProteinsCYP116B305Cytochrome P450Innot Hot Springs

Identifiers

PMID40450052
PMCPMC12126322

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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.