Evidence map›Paper›PMID 17117860›Full record

ArticleJournal of the American Chemical Society2006

X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior.

Michael S McCormick, Matthew H Sazinsky, Karen L Condon, Stephen J Lippard

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 43 citations in OpenAlex.

  1. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  2. Review
  3. Structure/function correlations over binuclear non-heme iron active sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Review
  4. Article
  5. Article
  6. Article
  7. Gates of enzymes.Chemical reviews · 2013
    Review
  8. Review
  9. Article
  10. Tracking a defined route for O₂ migration in a dioxygen-activating diiron enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Structural consequences of effector protein complex formation in a diiron hydroxylase.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Michael S McCormickDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Matthew H Sazinsky
Karen L Condon
Stephen J Lippard
Massachusetts Institute of Technology · US

Funding

NONHEME IRON AND THE BIOLOGICAL OXIDATION OF METHANER01GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J. · 1985 to 2013
$6.9M
LIGAND-BRIDGED POLYNUCLEAR METAL COMPLEXES &PROTEINSR37GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J · 1988 to 1997
–
NIGMS NIH HHS GM32134NIGMS NIH HHS R01 GM032134
6 · The paper itself

Abstract

We report the X-ray crystal structures of native and manganese(II)-reconstituted toluene/o-xylene monooxygenase hydroxylase (ToMOH) from Pseudomonas stutzeri OX1 to 1.85 and 2.20 A resolution, respectively. The structures reveal that reduction of the dimetallic active site is accompanied by a carboxylate shift and alteration of the coordination environment for dioxygen binding and activation. A rotamer shift in a strategically placed asparagine 202 accompanies dimetallic center reduction and is proposed to influence protein component interactions. This rotamer shift is conserved between ToMOH and the corresponding residue in methane monooxygenase hydroxylase (MMOH). Previously unidentified hydrophobic pockets similar to those present in MMOH are assigned.

Indexed as

Crystallography, X-RayManganeseModels, MolecularOxygenasesProtein ConformationManganesemethane monooxygenaseOxygenasestoluene 2-xylene monooxygenase

Identifiers

PMID17117860
PMCPMC1761687
OpenAlexW2063043621

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.