Molecular basis of enzymatic nitrogen-nitrogen formation by a family of zinc-binding cupin enzymes

Guiyun Zhao, Wei Peng, Kaihui Song, Jingkun Shi, Xingyu Lu, Binju Wang () and Yi-Ling Du ()
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Guiyun Zhao: Zhejiang University
Wei Peng: Xiamen University
Kaihui Song: Zhejiang University
Jingkun Shi: Zhejiang University
Xingyu Lu: Westlake University
Binju Wang: Xiamen University
Yi-Ling Du: Zhejiang University

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract Molecules with a nitrogen-nitrogen (N-N) bond in their structures exhibit various biological activities and other unique properties. A few microbial proteins are recently emerging as dedicated N-N bond forming enzymes in natural product biosynthesis. However, the details of these biochemical processes remain largely unknown. Here, through in vitro biochemical characterization and computational studies, we report the molecular basis of hydrazine bond formation by a family of di-domain enzymes. These enzymes are widespread in bacteria and sometimes naturally exist as two standalone enzymes. We reveal that the methionyl-tRNA synthase-like domain/protein catalyzes ATP-dependent condensation of two amino acids substrates to form a highly unstable ester intermediate, which is subsequently captured by the zinc-binding cupin domain/protein and undergoes redox-neutral intramolecular rearrangement to give the N-N bond containing product. These results provide important mechanistic insights into enzymatic N-N bond formation and should facilitate future development of novel N-N forming biocatalyst.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27523-x

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DOI: 10.1038/s41467-021-27523-x

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