Evidence map›Paper›PMID 21376009›Full record

ArticleArchives of biochemistry and biophysics2011

Cytochrome b₅ reductase-cytochrome b₅ as an active P450 redox enzyme system in Phanerochaete chrysosporium: atypical properties and in vivo evidence of electron transfer capability to CYP63A2.

Khajamohiddin Syed, Chandramohan Kattamuri, Thomas B Thompson, Jagjit S Yadav

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  3. Review
  4. A Cytochrome BFrontiers in plant science · 2021
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  7. Review
  8. Article
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  15. An injury-response mechanism conserved across kingdoms determines entry of the fungus Trichoderma atroviride into development.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

4 authors at 2 institutions in 1 country.

Khajamohiddin SyedEnvironmental Genetics and Molecular Toxicology Division, Department of Environmental Health, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0056, USA.
Chandramohan Kattamuri
Thomas B Thompson
Jagjit S Yadav
University of Cincinnati · USUniversity of Cincinnati Medical Center · US

Funding

FUNGAL P450 SYSTEMS IN BIODEGRADATION OF HIGHER PAHS-R01ES15543-01R01ES015543 · NIEHS · UNIVERSITY OF CINCINNATI · PI YADAV, JAGJIT S · 2008 to 2011
$1.1M
XENOBIOTIC-OXIDIZING P450 SYSTEM IN A WHITE ROT FUNGUSR01ES010210 · NIEHS · UNIVERSITY OF CINCINNATI · PI YADAV, JAGJIT S · 2001 to 2003
$689k
NIEHS NIH HHS R01 ES010210NIEHS NIH HHS R01 ES015543NIEHS NIH HHS R01 ES10210
6 · The paper itself

Abstract

Two central redox enzyme systems exist to reduce eukaryotic P450 enzymes, the P450 oxidoreductase (POR) and the cyt b₅ reductase-cyt b₅. In fungi, limited information is available for the cyt b(5) reductase-cyt b(5) system. Here we characterized the kinetic mechanism of (cyt b₅r)-cyt b₅ redox system from the model white-rot fungus Phanerochaete chrysosporium (Pc) and made a quantitative comparison to the POR system. We determined that Pc-cyt b₅r followed a "ping-pong" mechanism and could directly reduce cytochrome c. However, unlike other cyt b₅ reductases, Pc-cyt b₅r lacked the typical ferricyanide reduction activity, a standard for cyt b₅ reductases. Through co-expression in yeast, we demonstrated that the Pc-cyt b₅r-cyt b₅ complex is capable of transferring electrons to Pc-P450 CYP63A2 for its benzo(a)pyrene monooxygenation activity and that the efficiency was comparable to POR. In fact, both redox systems supported oxidation of an estimated one-third of the added benzo(a)pyrene amount. To our knowledge, this is the first report to indicate that the cyt b₅r-cyt b₅ complex of fungi is capable of transferring electrons to a P450 monooxygenase. Furthermore, this is the first eukaryotic quantitative comparison of the two P450 redox enzyme systems (POR and cyt b₅r-cyt b₅) in terms of supporting a P450 monooxygenase activity.

Indexed as

Cytochrome-B(5) ReductaseCytochrome P-450 Enzyme SystemCytochromes b5Electron TransportEscherichia coliGene ExpressionOxidation-ReductionPhanerochaetePichiaRecombinant ProteinsSubstrate SpecificityCytochrome-B(5) ReductaseCytochrome P-450 Enzyme SystemCytochromes b5Recombinant Proteins

Identifiers

PMID21376009
PMCPMC3119499
OpenAlexW1967612390

What OpenQuestion holds

Textmetadata
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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.