Evidence map›Paper›PMID 21591685›Full record

ArticleThe journal of physical chemistry. B2011

Bioelectronic delivery of electrons to cytochrome P450 enzymes.

Sadagopan Krishnan, John B Schenkman, James F Rusling

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 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

3 authors.

Sadagopan KrishnanDepartment of Chemistry, University of Connecticut, Storrs, Connecticut 06269, United States.
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 P450s (cyt P450s) are the major oxidative enzymes in human oxidative metabolism of drugs and xenobiotic chemicals. In nature, the iron heme cyt P450s utilize oxygen and electrons delivered from NADPH by a reductase enzyme to oxidize substrates stereo- and regioselectively. Significant research has been directed toward achieving these events electrochemically. This Feature Article discusses the direct electrochemistry of cyt P450s in thin films and the utilization of such films for electrochemically driven biocatalysis. Maintaining and confirming structural integrity and catalytic activity of cyt P450s in films is an essential feature of these efforts. We highlight here our efforts to elucidate the influence of iron heme spin state and secondary structure of human cyt P450s on voltammetric and biocatalytic properties, using methodologies to quantitatively describe the dynamics of these processes in thin films. We also describe the first cyt P450/reductase films that accurately mimic the natural biocatalytic pathway and show how they can be used with voltammetry to elucidate key mechanistic features. Such bioelectronic cyt P450 systems have high value for future drug development, toxicity screening, fundamental investigations, and chemical synthesis systems.

Indexed as

ElectronsElectron TransportBacterial ProteinsCytochrome P-450 Enzyme SystemElectrochemical TechniquesHumansModels, MolecularProtein ConformationSurface PropertiesBacterial ProteinsCytochrome P-450 Enzyme System

Identifiers

PMID21591685
PMCPMC3128182

What OpenQuestion holds

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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.