Evidence map›Paper›PMID 21167809›Full record

ReviewArchives of biochemistry and biophysics2011

Spectroscopic features of cytochrome P450 reaction intermediates.

Abhinav Luthra, Ilia G Denisov, Stephen G Sligar

Abstract readReview
In one paragraph

Review 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 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.9field-weighted citation impact, top 4% 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

66 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
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  7. Photooxidative molecular damage under blue light.Experimental & molecular medicine · 2026
    Review
  8. Article
  9. Article
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  12. Review
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  14. Article
  15. Non-Canonical Cytochrome P450 Enzymes in Nature.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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.

Abhinav LuthraDepartment of Biochemistry, School of Molecular and Cellular Biology, University of Illinois, Urbana, IL 61801, USA.
Ilia G Denisov
Stephen G Sligar
University of Illinois Urbana-Champaign · US

Funding

METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
HEME PROTEIN REDUCTASESR37GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1999 to 2008
$3.1M
HEME PROTEIN REDUCTASESR01GM031756 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2012
$1.5M
NIGMS NIH HHS GM31756NIGMS NIH HHS GM33775NIGMS NIH HHS R01 GM031756NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R37 GM031756
6 · The paper itself

Abstract

Cytochromes P450 constitute a broad class of heme monooxygenase enzymes with more than 11,500 isozymes which have been identified in organisms from all biological kingdoms [1]. These enzymes are responsible for catalyzing dozens chemical oxidative transformations such as hydroxylation, epoxidation, N-demethylation, etc., with very broad range of substrates [2,3]. Historically these enzymes received their name from 'pigment 450' due to the unusual position of the Soret band in UV-vis absorption spectra of the reduced CO-saturated state [4,5]. Despite detailed biochemical characterization of many isozymes, as well as later discoveries of other 'P450-like heme enzymes' such as nitric oxide synthase and chloroperoxidase, the phenomenological term 'cytochrome P450' is still commonly used as indicating an essential spectroscopic feature of the functionally active protein which is now known to be due to the presence of a thiolate ligand to the heme iron [6]. Heme proteins with an imidazole ligand such as myoglobin and hemoglobin as well as an inactive form of P450 are characterized by Soret maxima at 420nm [7]. This historical perspective highlights the importance of spectroscopic methods for biochemical studies in general, and especially for heme enzymes, where the presence of the heme iron and porphyrin macrocycle provides rich variety of specific spectroscopic markers available for monitoring chemical transformations and transitions between active intermediates of catalytic cycle.

Indexed as

AnimalsCircular DichroismCytochrome P-450 Enzyme SystemElectron Spin Resonance SpectroscopyHemeHumansNuclear Magnetic Resonance, BiomolecularSpectrophotometrySpectroscopy, MossbauerSpectrum AnalysisSpectrum Analysis, RamanX-Ray Absorption SpectroscopyCytochrome P-450 Enzyme SystemHeme

Identifiers

PMID21167809
PMCPMC3041835
OpenAlexW1965637904

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.