Evidence map›Paper›PMID 26299431›Full record

ArticleJournal of the American Chemical Society2015

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.

John A McIntosh, Thomas Heel, Andrew R Buller, Linda Chio, Frances H Arnold

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

14 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Electron Transfer Mechanism at the Interface of Multi-Heme Cytochromes and Metal Oxide.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  4. Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022
    Article
  5. Article
  6. Antibacterial Activity of Synthetic Cationic Iron Porphyrins.Antioxidants (Basel, Switzerland) · 2020
    Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Preface.Methods in enzymology · 2016
    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

5 authors at 1 institution in 1 country.

John A McIntoshDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Thomas HeelDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Andrew R BullerDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Linda ChioDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Frances H ArnoldDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
California Institute of Technology · US

Funding

Biocatalytic use of cytochrome P450 enzymesF32GM101792 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI MCINTOSH, JOHN ANDREW · 2012 to 2014
$150k
Radical SAM enzyme engineering to produce improved thiopeptide antibioticsF32GM110851 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BULLER, ANDREW · 2015 to 2016
$109k
Austrian Science Fund FWF J 3327NIGMS NIH HHS F32 GM101792NIGMS NIH HHS F32GM101792NIGMS NIH HHS F32 GM110851NIGMS NIH HHS F32GM110851
6 · The paper itself

Abstract

Almost all known members of the cytochrome P450 (CYP) superfamily conserve a key cysteine residue that coordinates the heme iron. Although mutation of this residue abolishes monooxygenase activity, recent work has shown that mutation to either serine or histidine unlocks non-natural carbene- and nitrene-transfer activities. Here we present the first crystal structure of a histidine-ligated P450. The T213A/C317H variant of the thermostable CYP119 from Sulfolobus acidocaldarius maintains heme iron coordination through the introduced ligand, an interaction that is accompanied by large changes in the overall protein structure. We also find that the axial cysteine C317 may be substituted with any other amino acid without abrogating folding and heme cofactor incorporation. Several of the axial mutants display unusual spectral features, suggesting that they have active sites with unique steric and electronic properties. These novel, highly stable enzyme active sites will be fruitful starting points for investigations of non-natural P450 catalysis and mechanisms.

Indexed as

Archaeal ProteinsCytochrome P-450 Enzyme SystemHemeHistidineModels, MolecularMutationProtein ConformationSulfolobus acidocaldariusArchaeal ProteinsCYP119 protein, Sulfolobus solfataricusCytochrome P-450 Enzyme SystemHemeHistidine

Identifiers

PMID26299431
PMCPMC4635421
OpenAlexW1766932748

What OpenQuestion holds

Textmetadata
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.