Evidence map›Paper›PMID 35933448›Full record

ArticleCommunications biology2022

Three pairs of surrogate redox partners comparison for Class I cytochrome P450 enzyme activity reconstitution.

Xiaohui Liu, Fengwei Li, Tianjian Sun, Jiawei Guo, Xingwang Zhang, Xianliang Zheng, Lei Du, Wei Zhang, Li Ma, Shengying Li

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Characterization of a CYP107 family vitamin DArchives of biochemistry and biophysics · 2026
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  11. Functional analysis, diversity, and distribution of theApplied and environmental microbiology · 2024
    Article
  12. Genomic insight intoHeliyon · 2024
    Article
  13. Designing cytochrome P450 enzymes for use in cancer gene therapy.Frontiers in bioengineering and biotechnology · 2024
    Review
  14. Article
  15. Article
  16. Article
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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

10 authors at 1 institution in 1 country.

Xiaohui Liu *State Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.
Fengwei Li *State Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.ORCID 0000-0002-7143-4151
Tianjian SunState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.
Jiawei GuoState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.
Xingwang ZhangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.ORCID 0000-0003-1346-1183
Xianliang ZhengCenter For Biocatalysis and Enzyme Technology, AngelYeast Co., Ltd., Cheng Dong Avenue, Yichang, Hubei, 443003, China.
Lei DuState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.
Wei ZhangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.
Li MaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China. maliqd@sdu.edu.cn.ORCID 0000-0003-1601-7125
Shengying LiState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong, 266237, China.ORCID 0000-0002-5244-870X
Shandong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most P450s require redox partners for the electron transfer during catalysis. However, little information is available on cognate redox partners for P450s, which greatly limits P450 function exploration and practical application. Thus, the stategy of building various hybrid P450 catalytic systems with surrogate redox partner has often adopted to engineer P450 biocatalysts. In this study, we compare three pairs of frequently-used surrogate redox partner SelFdx1499/SelFdR0978, Adx/AdR and Pdx/PdR and in terms of their electron transfer properties. The three selected bacterial Class I P450s include PikC, P450sca-2 and CYP-sb21, which are responsible for production of high-value-added products. Here we show that SelFdx1499/SelFdR0978 is the most promising redox partner compared to Adx/AdR and Pdx/PdR. The results provide insights into the domination for P450-redox partner interactions in modulating the catalytic activity of P450s. This study not only produces a more active biocatalyst but also suggests a general chose for a universal reductase which would facilitate engineering of P450 catalyst.

Indexed as

Cytochrome P-450 Enzyme SystemCatalysisElectron TransportOxidation-ReductionCytochrome P-450 Enzyme System

Identifiers

PMID35933448
PMCPMC9357085
OpenAlexW4289978012

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.