Praseodymium trivalent ion is an effective inhibitor of mitochondrial basic amino acids and carnitine/acylcarnitine carriers

Biochim Biophys Acta Bioenerg. 2022 Jun 1;1863(5):148557. doi: 10.1016/j.bbabio.2022.148557. Epub 2022 Apr 1.

Abstract

We herein report the identification of the lantanide praseodymium trivalent ion Pr3+ as inhibitor of mitochondrial transporters for basic amino acids and phylogenetically related carriers belonging to the Slc25 family. The inhibitory effect of Pr3+ has been tested using mitochondrial transporters reconstituted into liposomes being effective in the micromolar range, acting as a competitive inhibitor of the human basic amino acids carrier (BAC, Slc25A29), the human carnitine/acylcarnitine carrier (CAC, Slc25A20). Furthermore, we provide computational evidence that the complete inhibition of the transport activity of the recombinant proteins is due to the Pr3+ coordination to key acidic residues of the matrix salt bridge network. Besides being used as a first choice stop inhibitor for functional studies in vitro of mitochondrial carriers reconstituted in proteoliposomes, Pr3+ might also represent a useful tool for structural studies of the mitochondrial carrier family.

Keywords: Inhibitor; Liposomes; Mitochondria; Praseodymium; Reconstitution; Slc25 family transporters; Transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids, Basic
  • Carnitine / analogs & derivatives
  • Carnitine / metabolism
  • Carnitine Acyltransferases* / chemistry
  • Humans
  • Mitochondrial Membrane Transport Proteins / chemistry
  • Mitochondrial Proteins / metabolism
  • Praseodymium*

Substances

  • Amino Acids, Basic
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins
  • acylcarnitine
  • Carnitine Acyltransferases
  • SLC25A29 protein, human
  • Praseodymium
  • Carnitine