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. 2019 Jul 29;24(15):2743. doi: 10.3390/molecules24152743

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© 2019 by the author.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

(a) An artificial metalloenzyme constructed by replacement of the M-cluster with a synthesized [Fe₆S₉(SEt)₂]⁴⁻ cluster in nitrogenase scaffold. Reprinted with permission from [102]. Copyright 2015 Wiley-VCH; (b) The structure of [4Fe-4S(SCH₂CH₂OH)₄]²⁻ cluster (left), and its catalysis of CO₂/CO reduction in the presence of europium(II) diethylenetriaminepentaacetic acid (Eu^II-DTPA) (right) [104]. Copyright 2018 Nature press; (c) The proposed mechanism of l-cluster assembly in nitrogenase, followed by the maturation of M-cluster. SAM: S-adenosyl-l-methionine; NifH: the reductase component of Mo-nitrogenase;HC:homocitrate. Reprinted with permission from [103]. Copyright 2018 Macmillan Publishers.