Evidence map›Paper›PMID 21214177›Full record

ArticleJournal of the American Chemical Society2011

Efficient bioelectronic actuation of the natural catalytic pathway of human metabolic cytochrome P450s.

Sadagopan Krishnan, Dhanuka Wasalathanthri, Linlin Zhao, John B Schenkman, James F Rusling

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

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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

5 authors.

Sadagopan KrishnanDepartment of Chemistry, University of Connecticut, Storrs, Connecticut 06269, United States.
Dhanuka Wasalathanthri
Linlin Zhao
John B Schenkman
James F Rusling

Funding

ELECTROCATALYTIC STUDIES OF TOXIC POLLUTANT ACTIVATIONR01ES003154 · NIEHS · UNIVERSITY OF CONNECTICUT STORRS · PI RUSLING, JAMES F. · 1985 to 2018
$6.1M
NIEHS NIH HHS ES03154NIEHS NIH HHS R01 ES003154
6 · The paper itself

Abstract

Cytochrome (cyt) P450s comprise the enzyme superfamily responsible for human oxidative metabolism of a majority of drugs and xenobiotics. Electronic delivery of electrons to cyt P450s could be used to drive the natural catalytic cycle for fundamental investigations, stereo- and regioselective synthesis, and biosensors. We describe herein 30 nm nanometer-thick films on electrodes featuring excess human cyt P450s and cyt P450 reductase (CPR) microsomes that efficiently mimic the natural catalytic pathway for the first time. Redox potentials, electron-transfer rates, CO-binding, and substrate conversion rates confirmed that electrons are delivered from the electrode to CPR, which transfers them to cyt P450. The film system enabled electrochemical probing of the interaction between cyt P450 and CPR for the first time. Agreement of film voltammetry data with theoretical simulations supports a pathway featuring a key equilibrium redox reaction in the natural catalytic pathway between reduced CPR and cyt P450 occurring within a CPR-cyt P450 complex uniquely poised for substrate conversion.

Indexed as

BiocatalysisElectronsCarbon MonoxideCytochrome P-450 Enzyme SystemElectrochemistryElectrodesElectron TransportHumansKineticsMicrosomesNADPNADPH-Ferrihemoprotein ReductaseCarbon MonoxideCytochrome P-450 Enzyme SystemNADPNADPH-Ferrihemoprotein Reductase

Identifiers

PMID21214177
PMCPMC3033457

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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.