title: An open issue: the inner mitochondrial membrane (IMM) as a free boundary problem.
abstract: The inner mitochondrial membrane (IMM) is structured in cristae, which contributes to the best functioning of ions and adenylates exchange between the matrix and the intermembrane space. The central hypothesis of this paper is that the cristae structure favours a minimal mean free path of adenylates between translocation sites (translocase/ANT sites) and metabolic sites (ATPase sites). We propose a mathematical model and then give simulations. Based on simple hypotheses about cristae growth, they show that we can account for the major features of the IMM organization and functioning by minimizing the mean interdistance between ADP/ATP translocation and transformation sites.
authors.affiliation: TIMC-IMAG, UMR CNRS 5525, Faculty of Medicine, University J. Fourier, Domaine de la Merci, 38700 La Tronche, France. demongeo@mail-timc.imag.fr
authors.forename: Jacques
authors.initials: J
authors.lastname: Demongeot
authors.forename: Nicolas
authors.initials: N
authors.lastname: Glade
authors.forename: Olivier
authors.initials: O
authors.lastname: Hansen
authors.forename: Andrés
authors.initials: A
authors.lastname: Moreira
mesh_terms: D000227:Adenine Nucleotides / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000465:Algorithms; D001692:Biological Transport; D003198:Computer Simulation; D008854:Microscopy, Electron; D000226:Mitochondrial ADP, ATP Translocases / Q000378:metabolism; D051336:Mitochondrial Membranes / Q000378:metabolism* / Q000648:ultrastructure; D008954:Models, Biological
chemical_list: D000227:Adenine Nucleotides; D000226:Mitochondrial ADP, ATP Translocases; D000251:Adenosine Triphosphatases