Tools for resolving complexity in the electron transfer networks of multiheme cytochromes c
Metallomics, ISSN: 1756-5901, Vol: 3, Issue: 4, Page: 344-348
2011
- 43Citations
- 58Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations43
- Citation Indexes43
- 43
- CrossRef32
- Captures58
- Readers58
- 58
Article Description
Examining electron transfer between two proteins with identical spectroscopic signatures is a challenging task. It is supposed that several multiheme cytochromes in Shewanella oneidensis form a molecular "wire" through which electrons are transported across the cellular space and a direct study of this transient protein-protein interaction has not yet been reported. In this study, we present variations on catalytic protein film voltammetry and an anaerobic affinity chromatography assay to demonstrate unidirectional electron transfer between proposed protein pairs. Through use of these techniques, we are able to confirm the transient interactions between these cytochromes, supporting the model of electron transfer that is present in the literature. © The Royal Society of Chemistry.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79953797707&origin=inward; http://dx.doi.org/10.1039/c0mt00097c; http://www.ncbi.nlm.nih.gov/pubmed/21327265; https://academic.oup.com/metallomics/article/3/4/344-348/6016268; https://dx.doi.org/10.1039/c0mt00097c; https://academic.oup.com/metallomics/article-abstract/3/4/344/6016268?redirectedFrom=fulltext
Oxford University Press (OUP)
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know