Evidence map›Paper›PMID 28473297›Full record

ArticleBiochimica et biophysica acta. Proteins and proteomics2018

NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450.

Thomas C Pochapsky, Nathan Wong, Yihao Zhuang, Jeffrey Futcher, Maria-Eirini Pandelia, Drew R Teitz, Allison M Colthart

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Proteins and proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
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

7 authors at 1 institution in 1 country.

Thomas C PochapskyDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA. Electronic address: pochapsk@brandeis.edu.
Nathan WongDepartment of Biochemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA.
Yihao ZhuangDepartment of Biochemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA.
Jeffrey FutcherDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA.
Maria-Eirini PandeliaDepartment of Biochemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA.
Drew R TeitzDepartment of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA.
Allison M ColthartDepartment of Biochemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA.
Brandeis University · US

Funding

Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
STRUCTURE AND DYNAMICS OF METAL-CONTAINING PROTEINSR01GM044191 · NIGMS · BRANDEIS UNIVERSITY · PI POCHAPSKY, THOMAS CHARLES · 1995 to 2012
$3.4M
NIGMS NIH HHS R01 GM044191NIGMS NIH HHS T32 GM007596
6 · The paper itself

Abstract

The existence of a substrate-sensitive equilibrium between high spin (S=5/2) and low spin (S=1/2) ferric iron is a well-established phenomenon in the cytochrome P450 (CYP) superfamily, although its origins are still a subject of discussion. A series of mutations that strongly perturb the spin state equilibrium in the camphor hydroxylase CYP101A1 were recently described (Colthart et al., Sci. Rep. 6, 22035 (2016)). Wild type CYP101A1 as well as some CYP101A1 mutants are herein shown to be capable of catalyzing the reduction of nitroacetophenones by NADH to the corresponding anilino compounds (nitroreductase or NRase activity). The distinguishing characteristic between those mutants that catalyze the reduction and those that cannot appears to be the extent to which residual high spin form exists in the absence of the native substrate d-camphor, with those showing the largest spin state shifts upon camphor binding also exhibiting NRase activity. Optical and EPR spectroscopy was used to further examine these phenomena. These results suggest that reduction of nitroaromatics may provide a useful probe of residual high spin states in the CYP superfamily. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.

Indexed as

AcetophenonesAmino Acid MotifsBacterial ProteinsBinding SitesBiocatalysisCamphorCamphor 5-MonooxygenaseCloning, MolecularElectron Spin Resonance SpectroscopyEscherichia coliFerric CompoundsGene ExpressionHemeKineticsModels, MolecularNAD4-nitroacetophenoneAcetophenonesBacterial ProteinsCamphorCamphor 5-MonooxygenaseFerric CompoundsHemeNADRecombinant ProteinsElectron paramagnetic resonanceHeme proteinSubstrate recognition

Identifiers

PMID28473297
PMCPMC5665732
OpenAlexW2611430610

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.