Evidence map›Paper›PMID 37058990›Full record

ArticleJournal of inorganic biochemistry2023

Redox partner recognition and selectivity of cytochrome P450lin (CYP111A1).

Jessica A Gable, Thomas L Poulos, Alec H Follmer

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Jessica A GableDepartment of Chemistry, University of California, Irvine, Irvine, CA 92697-3900, USA.
Thomas L PoulosDepartment of Chemistry, University of California, Irvine, Irvine, CA 92697-3900, USA; Department of Molecular Biology & Biochemistry, University of California, Irvine, Irvine, CA 92697-3900, USA; Department of Pharmaceutical Sciences, University of California, Irvine, Irvine, CA 92697-3900, USA.
Alec H FollmerDepartment of Chemistry, University of California, Irvine, Irvine, CA 92697-3900, USA. Electronic address: afollmer@uci.edu.
University of California, Irvine · US

Funding

STRUCTURAL STUDIES ON NITRIC OXIDE SYNTHASER01GM057353 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI POULOS, THOMAS L · 1998 to 2018
$6.8M
Metalloenzyme structure, function, and as targets for neurodegeneration and bacterial pathogenesisR35GM131920 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI POULOS, THOMAS L · 2019 to 2023
$2.9M
Confining Metal Complexes within Protein Hosts: Models for Metalloprotein Active SitesR01GM120349 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI BOROVIK, ANDREW S. · 2017 to 2024
$2.4M
NIGMS NIH HHS R01 GM057353NIGMS NIH HHS R01 GM120349NIGMS NIH HHS R35 GM131920
6 · The paper itself

Abstract

The strict requirement of cytochrome P450cam for its native ferredoxin redox partner, putidaredoxin (Pdx), is not exhibited by any other known cytochrome P450 (CYP) system and the molecular details of redox partner selectivity are still not completely understood. We therefore examined the selectivity of a related Pseudomonas cytochrome P450, P450lin, by testing its activity with non-native redox partners. We found that P450lin could utilize Arx, the native redox partner of CYP101D1, to enable turnover of its substrate, linalool, while Pdx showed limited activity. Arx exhibited a higher sequence similarity to P450lins native redox partner, linredoxin (Ldx) than Pdx, including several residues that are believed to be at the interface of the two proteins, based on the P450cam-Pdx complex structure. We therefore mutated Pdx to resemble Ldx and Arx and found that a double mutant, D38L/∆106, displayed higher activity than Arx. In addition, Pdx D38L/∆106 does not induce a low-spin shift in linalool bound P450lin but does destabilize the P450lin-oxycomplex. Together our results suggest that P450lin and its redox partners may form a similar interface to P450cam-Pdx, but the interactions that allow for productive turnover are different.

Indexed as

Camphor 5-MonooxygenasePseudomonas putidaAcyclic MonoterpenesCytochrome P-450 Enzyme SystemFerredoxinsOxidation-ReductionAcyclic MonoterpenesCamphor 5-MonooxygenaseCytochrome P-450 Enzyme SystemFerredoxinslinaloolCytochrome P450electron transferFerredoxinsProtein-protein interactionsRedox partnersStopped-flow

Identifiers

PMID37058990
PMCPMC10519177
OpenAlexW4362696506

What OpenQuestion holds

Textmetadata
LicenceTDM
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.