Evidence map›Paper›PMID 18174331›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative.

Martin Newcomb, James A Halgrimson, John H Horner, Erik C Wasinger, Lin X Chen, Stephen G Sligar

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Heme-copper and Heme OJournal of inorganic biochemistry · 2023
    Review
  3. Article
  4. Article
  5. Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Review
  6. Heme-FeJournal of the American Chemical Society · 2020
    Article
  7. Article
  8. Article
  9. Mechanistic insight from thermal activation parameters for oxygenation reactions of different substrates with biomimetic iron porphyrin models for compounds I and II.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  10. Article
  11. Article
  12. Nature of the ferryl heme in compounds I and II.The Journal of biological chemistry · 2011
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

6 authors.

Martin NewcombDepartment of Chemistry, University of Illinois, 845 West Taylor Street, Chicago, IL 60607, USA. men@uic.edu
James A Halgrimson
John H Horner
Erik C Wasinger
Lin X Chen
Stephen G Sligar

Funding

MECHANISTIC PROBES FOR ENZYME-CATALYZED OXIDATIONSR01GM048722 · NIGMS · WAYNE STATE UNIVERSITY · PI NEWCOMB, MARTIN E · 1993 to 2010
$2.6M
NIGMS NIH HHS GM-48722NIGMS NIH HHS R01 GM048722
6 · The paper itself

Abstract

The cytochrome P450 enzyme CYP119, its compound II derivative, and its nitrosyl complex were studied by iron K-edge x-ray absorption spectroscopy. The compound II derivative was prepared by reaction of the resting enzyme with peroxynitrite and had a lifetime of approximately 10 s at 23 degrees C. The CYP119 nitrosyl complex was prepared by reaction of the enzyme with nitrogen monoxide gas or with a nitrosyl donor and was stable at 23 degrees C for hours. Samples of CYP119 and its derivatives were studied by x-ray absorption spectroscopy at temperatures below 140 (K) at the Advanced Photon Source of Argonne National Laboratory. The x-ray absorption near-edge structure spectra displayed shifts in edge and pre-edge energies consistent with increasing effective positive charge on iron in the series native CYP119 < CYP119 nitrosyl complex < CYP119 compound II derivative. Extended x-ray absorption fine structure spectra were simulated with good fits for k = 12 A(-1) for native CYP119 and k = 13 A(-1) for both the nitrosyl complex and the compound II derivative. The important structural features for the compound II derivative were an iron-oxygen bond length of 1.82 A and an iron-sulfur bond length of 2.24 A, both of which indicate an iron-oxygen single bond in a ferryl-hydroxide, Fe(IV)OH, moiety.

Indexed as

Absorptiometry, PhotonArchaeal ProteinsCytochrome P-450 Enzyme SystemIronNitric OxidePeroxynitrous AcidPorphyrinsReactive Oxygen SpeciesArchaeal ProteinsCYP119 protein, Sulfolobus solfataricusCytochrome P-450 Enzyme SystemIronNitric OxidePeroxynitrous AcidPorphyrinsReactive Oxygen Species

Identifiers

PMID18174331
PMCPMC2448811

What OpenQuestion holds

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Registered trials

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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.