A model for metalloprotein-catalysed ADP, ATP transport in mitochondria.
We propose a hypothetical model for the transmembrane exchange reaction catalysed by the mitochondrial adenine nucleotide carrier protein, which basically consists of an alternating reorientation of a transitory carrier-metal-nucleotide complex. The key features of the model are: the participation of an intrinsic divalent metal ion in the course of transport catalysis; the different stability constants of protonated and deprotonated nucleotide-metal complexes; the exposure and retraction of strategic arginyl residues; the alternating reorientation of the active center involving a change from the cytosolic conformation (Cc) to the matrix conformation (Cm).
D000818:Animals; D001665:Binding Sites; D003600:Cytosol / Q000378:metabolism; D004579:Electron Transport; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008667:Metalloproteins / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology*; D000226:Mitochondrial ADP, ATP Translocases / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D008968:Molecular Conformation; D009713:Nucleotidyltransferases / Q000378:metabolism*; D011485:Protein Binding
D008667:Metalloproteins; D000226:Mitochondrial ADP, ATP Translocases; D009713:Nucleotidyltransferases