期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 7, 期 21, 页码 4427-4432出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.6b02061
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资金
- National Natural Science Foundation of China (NSFC) [21290194, 21521062, 21473215]
- Institute of Chemistry, Chinese Academy of Sciences
Cyanobacterial aldehyde-deformylating oxygenase (cADO) is a nonheme diiron enzyme that catalyzes the conversion of aldehyde to alk(a/e)ne, an important transformation in biofuel research. In this work, we report a highly desired computational study for probing the mechanism of cADO. By combining our QM/MM results with the available Fe-57 Mossbauer spectroscopic data, the gained detailed structural information suggests construction of asymmetry from the symmetric diiron cofactor in an aldehyde substrate and O-2 activation. His(160), one of the two iron-coordinate histidine residues in cADO, plays a pivotal role in this asymmetric aldehyde activation process by unprecedented reversible dissociation from the diiron cofactor, a behavior unknown in any other nonheme dinuclear or mononuclear enzymes. The revealed intrinsically asymmetric interactions of the substrate/O-2 with the symmetric cofactor in cADO are inspirational for exploring diiron subsite resolution in other nonheme diiron enzymes.
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