Biological Pincer Complexes
- 8 May 2020
- journal article
- review article
- Published by Wiley in ChemCatChem
- Vol. 12 (17) , 4242-4254
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.Keywords
Funding Information
- National Science Foundation (CHE1807073)
- National Institutes of Health (GM128959)
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