H2O2, O2, and C-H Activation by Artificial Copper Proteins (ArCuPs)
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Sandeep Misra
LAB HEAD: Sandeep Misra
PROVIDER: PXD061034 | Pride | 2026-06-01
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| 3SCC-Cu-H2O2-1.raw | Raw | |||
| 3SCC-Cu-H2O2-1.xlsx | Xlsx | |||
| 3SCC-Cu-H2O2-2.raw | Raw | |||
| 3SCC-Cu-H2O2-2.xlsx | Xlsx | |||
| 3SCC-Cu-H2O2-3.raw | Raw |
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Publications
Mechanism of Oxidative C─H Bond Activation by De Novo Designed Artificial Cu Metalloenzymes Using H<sub>2</sub>O<sub>2</sub> and O<sub>2</sub>.
Prakash Divyansh D Wu Yao Y Misra Sandeep K SK Sampath Nishanthini N Wang Binju B Chakraborty Saumen S
Chemistry (Weinheim an der Bergstrasse, Germany) 20250813 52
De novo-designed artificial Cu protein (ArCuP), 3SCC, featuring a trigonal Cu(His)<sub>3</sub> binding environment, activates H<sub>2</sub>O<sub>2</sub>, O<sub>2</sub>, and benzylic C─H bonds of abiotic substrates. We outline the mechanism of ArCuP-catalyzed C─H peroxidation of one such abiotic substrate, the peroxidation of benzyl alcohol (BA) to benzaldehyde. The Cu<sup>I</sup>(H<sub>2</sub>O<sub>2</sub>) complex undergoes homolytic cleavage, producing Cu<sup>II</sup>-OH and <sup>•</sup>OH, ak ...[more]
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