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Intermediates in the transformation of phosphonates to phosphate by bacteria

Overview of attention for article published in Nature, November 2011
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (91st percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

blogs
1 blog
twitter
3 tweeters
wikipedia
4 Wikipedia pages
f1000
1 research highlight platform

Citations

dimensions_citation
81 Dimensions

Readers on

mendeley
133 Mendeley
citeulike
1 CiteULike
Title
Intermediates in the transformation of phosphonates to phosphate by bacteria
Published in
Nature, November 2011
DOI 10.1038/nature10622
Pubmed ID
Authors

Siddhesh S. Kamat, Howard J. Williams, Frank M. Raushel

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.

Twitter Demographics

The data shown below were collected from the profiles of 3 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 133 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 5 4%
Australia 1 <1%
France 1 <1%
Austria 1 <1%
Netherlands 1 <1%
United Kingdom 1 <1%
Canada 1 <1%
Mexico 1 <1%
Switzerland 1 <1%
Other 0 0%
Unknown 120 90%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 37 28%
Student > Master 18 14%
Researcher 17 13%
Student > Bachelor 12 9%
Professor > Associate Professor 10 8%
Other 23 17%
Unknown 16 12%
Readers by discipline Count As %
Agricultural and Biological Sciences 48 36%
Chemistry 21 16%
Biochemistry, Genetics and Molecular Biology 15 11%
Environmental Science 10 8%
Earth and Planetary Sciences 6 5%
Other 17 13%
Unknown 16 12%

Attention Score in Context

This research output has an Altmetric Attention Score of 15. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 23 February 2015.
All research outputs
#1,562,733
of 17,351,915 outputs
Outputs from Nature
#35,589
of 79,621 outputs
Outputs of similar age
#7,775
of 96,306 outputs
Outputs of similar age from Nature
#436
of 696 outputs
Altmetric has tracked 17,351,915 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 90th percentile: it's in the top 10% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 79,621 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 89.4. This one has gotten more attention than average, scoring higher than 55% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 96,306 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 91% of its contemporaries.
We're also able to compare this research output to 696 others from the same source and published within six weeks on either side of this one. This one is in the 37th percentile – i.e., 37% of its contemporaries scored the same or lower than it.