Cobaloxime-based artificial hydrogenases
Inorganic Chemistry, ISSN: 1520-510X, Vol: 53, Issue: 15, Page: 8071-8082
2014
- 79Citations
- 66Captures
- 1Mentions
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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
- Citations79
- Citation Indexes79
- 79
- CrossRef77
- Captures66
- Readers66
- 66
- Mentions1
- News Mentions1
- News1
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Hydrogen Evolution from Water under Aerobic Conditions Catalyzed by a Cobalt ATCUN Metallopeptide
Hydrogen is touted as an energy-dense carbon-free fuel; however, most hydrogen is currently produced via steam reforming of hydrocarbons. (1) A potentially more sustainable route
Article Description
Cobaloximes are popular H evolution molecular catalysts but have so far mainly been studied in nonaqueous conditions. We show here that they are also valuable for the design of artificial hydrogenases for application in neutral aqueous solutions and report on the preparation of two well-defined biohybrid species via the binding of two cobaloxime moieties, {Co(dmgH) } and {Co(dmgBF)} (dmgH = dimethylglyoxime), to apo Sperm-whale myoglobin (SwMb). All spectroscopic data confirm that the cobaloxime moieties are inserted within the binding pocket of the SwMb protein and are coordinated to a histidine residue in the axial position of the cobalt complex, resulting in thermodynamically stable complexes. Quantum chemical/molecular mechanical docking calculations indicated a coordination preference for His93 over the other histidine residue (His64) present in the vicinity. Interestingly, the redox activity of the cobalt centers is retained in both biohybrids, which provides them with the catalytic activity for H evolution in near-neutral aqueous conditions. © 2014 American Chemical Society.
Bibliographic Details
American Chemical Society (ACS)
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