↓ Skip to main content

Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron–electron resonance

Overview of attention for article published in Proceedings of the National Academy of Sciences of the United States of America, January 2010
Altmetric Badge

Mentioned by

wikipedia
3 Wikipedia pages

Readers on

mendeley
124 Mendeley
citeulike
1 CiteULike
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron–electron resonance
Published in
Proceedings of the National Academy of Sciences of the United States of America, January 2010
DOI 10.1073/pnas.0908050107
Pubmed ID
Authors

Maxie M. Roessler, Martin S. King, Alan J. Robinson, Fraser A. Armstrong, Jeffrey Harmer, Judy Hirst

Abstract

In oxidative phosphorylation, complex I (NADH:quinone oxidoreductase) couples electron transfer to proton translocation across an energy-transducing membrane. Complex I contains a flavin mononucleotide to oxidize NADH, and an unusually long series of iron-sulfur (FeS) clusters, in several subunits, to transfer the electrons to quinone. Understanding coupled electron transfer in complex I requires a detailed knowledge of the properties of individual clusters and of the cluster ensemble, and so it requires the correlation of spectroscopic and structural data: This has proved a challenging task. EPR studies on complex I from Bos taurus have established that EPR signals N1b, N2 and N3 arise, respectively, from the 2Fe cluster in the 75 kDa subunit, and from 4Fe clusters in the PSST and 51 kDa subunits (positions 2, 7, and 1 along the seven-cluster chain extending from the flavin). The other clusters have either evaded detection or definitive signal assignments have not been established. Here, we combine double electron-electron resonance (DEER) spectroscopy on B. taurus complex I with the structure of the hydrophilic domain of Thermus thermophilus complex I. By considering the magnetic moments of the clusters and the orientation selectivity of the DEER experiment explicitly, signal N4 is assigned to the first 4Fe cluster in the TYKY subunit (position 5), and N5 to the all-cysteine ligated 4Fe cluster in the 75 kDa subunit (position 3). The implications of our assignment for the mechanisms of electron transfer and energy transduction by complex I are discussed.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 124 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 3 2%
Japan 1 <1%
United States 1 <1%
Italy 1 <1%
Unknown 118 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 27 22%
Researcher 27 22%
Student > Master 14 11%
Student > Bachelor 9 7%
Student > Doctoral Student 8 6%
Other 20 16%
Unknown 19 15%
Readers by discipline Count As %
Chemistry 36 29%
Agricultural and Biological Sciences 27 22%
Biochemistry, Genetics and Molecular Biology 27 22%
Physics and Astronomy 5 4%
Pharmacology, Toxicology and Pharmaceutical Science 1 <1%
Other 5 4%
Unknown 23 19%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. 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 17 January 2019.
All research outputs
#8,882,501
of 26,017,215 outputs
Outputs from Proceedings of the National Academy of Sciences of the United States of America
#67,601
of 104,451 outputs
Outputs of similar age
#53,232
of 178,040 outputs
Outputs of similar age from Proceedings of the National Academy of Sciences of the United States of America
#603
of 875 outputs
Altmetric has tracked 26,017,215 research outputs across all sources so far. This one is in the 42nd percentile – i.e., 42% of other outputs scored the same or lower than it.
So far Altmetric has tracked 104,451 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 39.5. This one is in the 14th percentile – i.e., 14% of its peers scored the same or lower than it.
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 178,040 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 19th percentile – i.e., 19% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 875 others from the same source and published within six weeks on either side of this one. This one is in the 13th percentile – i.e., 13% of its contemporaries scored the same or lower than it.