Evidence map›Paper›PMID 22089136›Full record

ArticleNature2011

Intermediates in the transformation of phosphonates to phosphate by bacteria.

Siddhesh S Kamat, Howard J Williams, Frank M Raushel

Abstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.7field-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

59 citing papers in PubMed, 151 citations in OpenAlex.

  1. Applied and environmental microbiology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Phosphonate-driven oxic CHISME communications · 2025
    Article
  8. Review
  9. Article
  10. Laundry IsolateMicroorganisms · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Nano Ag/CoPolymers · 2022
    Article
  17. Article
  18. Article
  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

3 authors at 1 institution in 1 country.

Siddhesh S KamatDepartment of Chemistry, PO Box 30012, Texas A&M University, College Station, Texas 77843, USA.
Howard J Williams
Frank M Raushel
Texas A&M University · US

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI CRONAN, JOHN E. · 2010 to 2015
$34.6M
Theoretical and Computational ApproachesP01GM071790 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RAUSHEL, FRANK M. · 2004 to 2013
$15.5M
NIGMS NIH HHS GM71790NIGMS NIH HHS GM93342NIGMS NIH HHS P01 GM071790NIGMS NIH HHS U54 GM093342
6 · The paper itself

Abstract

Phosphorus is an essential element for all known forms of life. In living systems, phosphorus is an integral component of nucleic acids, carbohydrates and phospholipids, where it is incorporated as a derivative of phosphate. However, most Gram-negative bacteria have the capability to use phosphonates as a nutritional source of phosphorus under conditions of phosphate starvation. In these organisms, methylphosphonate is converted to phosphate and methane. In a formal sense, this transformation is a hydrolytic cleavage of a carbon-phosphorus (C-P) bond, but a general enzymatic mechanism for the activation and conversion of alkylphosphonates to phosphate and an alkane has not been elucidated despite much effort for more than two decades. The actual mechanism for C-P bond cleavage is likely to be a radical-based transformation. In Escherichia coli, the catalytic machinery for the C-P lyase reaction has been localized to the phn gene cluster. This operon consists of the 14 genes phnC, phnD, …, phnP. Genetic and biochemical experiments have demonstrated that the genes phnG, phnH, …, phnM encode proteins that are essential for the conversion of phosphonates to phosphate and that the proteins encoded by the other genes in the operon have auxiliary functions. There are no functional annotations for any of the seven proteins considered essential for C-P bond cleavage. Here we show that methylphosphonate reacts with MgATP to form α-D-ribose-1-methylphosphonate-5-triphosphate (RPnTP) and adenine. The triphosphate moiety of RPnTP is hydrolysed to pyrophosphate and α-D-ribose-1-methylphosphonate-5-phosphate (PRPn). The C-P bond of PRPn is subsequently cleaved in a radical-based reaction producing α-D-ribose-1,2-cyclic-phosphate-5-phosphate and methane in the presence of S-adenosyl-L-methionine. Substantial quantities of phosphonates are produced worldwide for industrial processes, detergents, herbicides and pharmaceuticals. Our elucidation of the chemical steps for the biodegradation of alkylphosphonates shows how these compounds can be metabolized and recycled to phosphate.

Indexed as

Escherichia coliEscherichia coli ProteinsLyasesOrganophosphonatesPhosphatesEscherichia coli ProteinsLyasesOrganophosphonatesPhosphates

Identifiers

PMID22089136
PMCPMC3245791
OpenAlexW2040705798

What OpenQuestion holds

Textmetadata
LicenceTDM
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.