Biological Pincer Complexes. Issue 17 (24th June 2020)

• Record Type: Journal Article
• Authors: Nevarez, Jorge L.; Turmo, Aiko; Hu, Jian; Hausinger, Robert P.
• Is Part Of: ChemCatChem. Volume 12:Issue 17(2020)
• Page Start: 4242
• Page End: 4254
• Publication Date: 2020-06-24
• Subjects: metalloenzyme -- cofactor -- nickel -- biosynthesis -- biocatalysis; Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.202000575
• Languages: English
• ISSNs: 1867-3880

Abstract

Abstract: At least two types of pincer complexes are known to exist in biology. A metal‐pyrroloquinolone quinone (PQQ) cofactor was first identified in bacterial methanol dehydrogenase, and later also found in selected short‐chain alcohol dehydrogenases of other microorganisms. The PQQ‐associated metal can be calcium, magnesium, or a rare earth element depending on the enzyme sequence. Synthesis of this organic ligand requires a series of accessory proteins acting on a small peptide, PqqA. Binding of metal to PQQ yields an ONO‐type pincer complex. More recently, a nickel‐pincer nucleotide (NPN) cofactor was discovered in lactate racemase, LarA. This cofactor derives from nicotinic acid adenine dinucleotide via action of a carboxylase/hydrolase, sulfur transferase, and nickel insertase, resulting in an SCS‐type pincer complex. The NPN cofactor likely occurs in selected other racemases and epimerases of bacteria, archaea, and a few eukaryotes. Abstract : It's natural : Biological representatives of metal‐pincer complexes include pyrroloquinoline quinone bound to calcium, magnesium, or lanthanide metals (M‐PQQ) in selected dehydrogenases and nickel‐pincer nucleotide (Ni‐NPN) cofactors of certain racemases and epimerases.