Evidence map›Paper›PMID 19588962›Full record

ArticleJournal of the American Chemical Society2009

Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.

Megan J Hawk, Robert M Breece, Christine E Hajdin, Katherine M Bender, Zhenxin Hu, Alison L Costello, Brian Bennett, David L Tierney, Michael W Crowder

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Metallo-ß-lactamases: a review.Molecular biology reports · 2020
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Metallo-β-lactamase structure and function.Annals of the New York Academy of Sciences · 2013
    Review
  16. Article
  17. Article
  18. 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

9 authors.

Megan J HawkDepartment of Chemistry and Biochemistry, 160 Hughes Hall, Miami University, Oxford, Ohio 45056, USA.
Robert M Breece
Christine E Hajdin
Katherine M Bender
Zhenxin Hu
Alison L Costello
Brian Bennett
David L Tierney
Michael W Crowder

Funding

ZUNI HEALTH INITIATIVE-PILOT STUDYP20RR016480 · NCRR · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI FENG, CHANGJIAN · 2001 to 2011
$33.7M
TR&D Project 3P41EB001980 · NIBIB · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S · 2003 to 2017
$16.3M
Substrate &Inhibitor Binding in Leucine AminopeptidaseR01AI056231 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI BENNETT, BRIAN · 2003 to 2007
$923k
NCRR NIH HHS P20 RR016480NCRR NIH HHS RR16480NIAID NIH HHS AI056231NIAID NIH HHS R01 AI056231NIBIB NIH HHS EB001980NIBIB NIH HHS P41 EB001980
6 · The paper itself

Abstract

In an effort to probe the structure, mechanism, and biochemical properties of metallo-beta-lactamase Bla2 from Bacillus anthracis, the enzyme was overexpressed, purified, and characterized. Metal analyses demonstrated that recombinant Bla2 tightly binds 1 equiv of Zn(II). Steady-state kinetic studies showed that mono-Zn(II) Bla2 (1Zn-Bla2) is active, while di-Zn(II) Bla2 (ZnZn-Bla2) was unstable. Catalytically, 1Zn-Bla2 behaves like the related enzymes CcrA and L1. In contrast, di-Co(II) Bla2 (CoCo-Bla2) is substantially more active than the mono-Co(II) analogue. Rapid kinetics and UV-vis, (1)H NMR, EPR, and EXAFS spectroscopic studies show that Co(II) binding to Bla2 is distributed, while EXAFS shows that Zn(II) binding is sequential. To our knowledge, this is the first documented example of a Zn enzyme that binds Co(II) and Zn(II) via distinct mechanisms, underscoring the need to demonstrate transferability when extrapolating results on Co(II)-substituted proteins to the native Zn(II)-containing forms.

Indexed as

Bacillus anthracisbeta-LactamasesCobaltKineticsProtein BindingRecombinant ProteinsSpectrum AnalysisSubstrate SpecificityZincbeta-LactamasesCobaltRecombinant ProteinsZinc

Identifiers

PMID19588962
PMCPMC3295577

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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.