Encapsulating [FeFe]-hydrogenase model compounds in peptide hydrogels dramatically modifies stability and photochemistry
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2012/DT/C2DT30307H
Reference46 articles.
1. Insights into [FeFe]-Hydrogenase Structure, Mechanism, and Maturation
2. Structural and Functional Analogues of the Active Sites of the [Fe]-, [NiFe]-, and [FeFe]-Hydrogenases
3. Spectroscopically characterized intermediates of catalytic H2 formation by [FeFe] hydrogenase models
4. Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity
5. Artificial [FeFe]‐Hydrogenase: On Resin Modification of an Amino Acid to Anchor a Hexacarbonyldiiron Cluster in a Peptide Framework
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1. Bioinspired functional self-healing hydrogels from a minimalistic dipeptide building block;Journal of Materials Chemistry A;2024
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3. Peptide self‐assembly as a strategy for facile immobilization of redox enzymes on carbon electrodes;Carbon Energy;2023-07-11
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