5ON9

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

5ON9 の概要

• エントリーDOI: 10.2210/pdb5on9/pdb
• 分子名称: Nickel-binding periplasmic protein, FE (III) ION, 2-[2-[2-hydroxy-2-oxoethyl-[(3-methoxy-2-oxidanyl-phenyl)methyl]amino]ethyl-[(2-methylsulfanylphenyl)methyl]amino]ethanoic acid, ... (8 entities in total)
• 機能のキーワード: artificial oxygenase, clec, dioxygen activation, oxidation of carbon-carbon double bonds, metal binding protein
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115198.24

構造登録者

Cavazza, C.,Menage, S. (登録日: 2017-08-03, 公開日: 2017-12-13, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)