The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein
Dalton Transactions, ISSN: 1477-9234, Vol: 49, Issue: 6, Page: 1928-1934
2020
- 7Captures
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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
- Captures7
- Readers7
Article Description
The O reactivity of an artificial biomolecular hydrogenase, the nickel binding protein (NBP) is investigated. Kinetic analyses revealed a complete 4e reduction of O to HO under catalytic conditions with associated k for ET in the order of 10 cm s. Protein destabilization and S oxygenation are contributing factors to the deactivation of NBP under oxic conditions. Computational studies provided insight into the S oxygenation and the reaction intermediates of a proposed mechanistic pathway for O activation by NBP.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85079248030&origin=inward; http://dx.doi.org/10.1039/c9dt04913d; http://www.ncbi.nlm.nih.gov/pubmed/31971173; https://xlink.rsc.org/?DOI=C9DT04913D; https://dx.doi.org/10.1039/c9dt04913d; https://pubs.rsc.org/en/content/articlelanding/2020/dt/c9dt04913d
Royal Society of Chemistry (RSC)
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