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PNAS

Negative cooperativity in the nitrogenase Fe protein electron delivery cycle

Overview of attention for article published in Proceedings of the National Academy of Sciences of the United States of America, October 2016
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  • In the top 5% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (95th percentile)
  • Good Attention Score compared to outputs of the same age and source (74th percentile)

Mentioned by

news
8 news outlets
blogs
1 blog

Citations

dimensions_citation
39 Dimensions

Readers on

mendeley
102 Mendeley
citeulike
1 CiteULike
Title
Negative cooperativity in the nitrogenase Fe protein electron delivery cycle
Published in
Proceedings of the National Academy of Sciences of the United States of America, October 2016
DOI 10.1073/pnas.1613089113
Pubmed ID
Authors

Karamatullah Danyal, Sudipta Shaw, Taylor R Page, Simon Duval, Masaki Horitani, Amy R Marts, Dmitriy Lukoyanov, Dennis R Dean, Simone Raugei, Brian M Hoffman, Lance C Seefeldt, Edwin Antony

Abstract

Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to two ammonia (NH3) molecules through the participation of its two protein components, the MoFe and Fe proteins. Electron transfer (ET) from the Fe protein to the catalytic MoFe protein involves a series of synchronized events requiring the transient association of one Fe protein with each αβ half of the α2β2 MoFe protein. This process is referred to as the Fe protein cycle and includes binding of two ATP to an Fe protein, association of an Fe protein with the MoFe protein, ET from the Fe protein to the MoFe protein, hydrolysis of the two ATP to two ADP and two Pi for each ET, Pi release, and dissociation of oxidized Fe protein-(ADP)2 from the MoFe protein. Because the MoFe protein tetramer has two separate αβ active units, it participates in two distinct Fe protein cycles. Quantitative kinetic measurements of ET, ATP hydrolysis, and Pi release during the presteady-state phase of electron delivery demonstrate that the two halves of the ternary complex between the MoFe protein and two reduced Fe protein-(ATP)2 do not undergo the Fe protein cycle independently. Instead, the data are globally fit with a two-branch negative-cooperativity kinetic model in which ET in one-half of the complex partially suppresses this process in the other. A possible mechanism for communication between the two halves of the nitrogenase complex is suggested by normal-mode calculations showing correlated and anticorrelated motions between the two halves.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 102 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 <1%
Netherlands 1 <1%
Unknown 100 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 28 27%
Researcher 18 18%
Student > Master 10 10%
Student > Bachelor 9 9%
Student > Doctoral Student 7 7%
Other 12 12%
Unknown 18 18%
Readers by discipline Count As %
Chemistry 28 27%
Biochemistry, Genetics and Molecular Biology 23 23%
Agricultural and Biological Sciences 16 16%
Environmental Science 3 3%
Chemical Engineering 2 2%
Other 9 9%
Unknown 21 21%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 60. 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 06 October 2016.
All research outputs
#677,958
of 24,629,540 outputs
Outputs from Proceedings of the National Academy of Sciences of the United States of America
#11,528
of 101,529 outputs
Outputs of similar age
#13,270
of 327,497 outputs
Outputs of similar age from Proceedings of the National Academy of Sciences of the United States of America
#260
of 1,005 outputs
Altmetric has tracked 24,629,540 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 97th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 101,529 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 38.8. This one has done well, scoring higher than 88% 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 327,497 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 95% of its contemporaries.
We're also able to compare this research output to 1,005 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 74% of its contemporaries.