5ON4

Crystal structure of NikA in complex with Fe-L1 (N-(2-hydroxybenzyl)-N'-(2-thiomethylbenzyl)-N,N'-ethylenediamine diacetic acid)

Summary for 5ON4

• Entry DOI: 10.2210/pdb5on4/pdb
• Descriptor: Nickel-binding periplasmic protein, FE (III) ION, 2-[2-[[2,3-bis(oxidanyl)phenyl]methyl-(2-hydroxy-2-oxoethyl)amino]ethyl-[(2-methylsulfanylphenyl)methyl]amino]ethanoic acid, ... (5 entities in total)
• Functional Keywords: artificial oxygenase, clec, dioxygen activation, oxidation of carbon-carbon double bonds, metal binding protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 114070.55

Authors

Cavazza, C.,Menage, S. (deposition date: 2017-08-02, release date: 2017-12-13, Last modification date: 2024-01-17)

Primary citation

Lopez, S.,Rondot, L.,Lepretre, C.,Marchi-Delapierre, C.,Menage, S.,Cavazza, C.
Cross-Linked Artificial Enzyme Crystals as Heterogeneous Catalysts for Oxidation Reactions.
J. Am. Chem. Soc., 139:17994-18002, 2017

PubMed Abstract: Designing systems that merge the advantages of heterogeneous catalysis, enzymology, and molecular catalysis represents the next major goal for sustainable chemistry. Cross-linked enzyme crystals display most of these essential assets (well-designed mesoporous support, protein selectivity, and molecular recognition of substrates). Nevertheless, a lack of reaction diversity, particularly in the field of oxidation, remains a constraint for their increased use in the field. Here, thanks to the design of cross-linked artificial nonheme iron oxygenase crystals, we filled this gap by developing biobased heterogeneous catalysts capable of oxidizing carbon-carbon double bonds. First, reductive O activation induces selective oxidative cleavage, revealing the indestructible character of the solid catalyst (at least 30 000 turnover numbers without any loss of activity). Second, the use of 2-electron oxidants allows selective and high-efficiency hydroxychlorination with thousands of turnover numbers. This new technology by far outperforms catalysis using the inorganic complexes alone, or even the artificial enzymes in solution. The combination of easy catalyst synthesis, the improvement of "omic" technologies, and automation of protein crystallization makes this strategy a real opportunity for the future of (bio)catalysis.

PubMed: 29148757
DOI: 10.1021/jacs.7b09343

Experimental method

X-RAY DIFFRACTION (2.3 Å)