All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Exploring the proton transport mechanism of the mitochondrial ADP/ATP carrier: FA-cycling hypothesis and beyond

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F25%3A43933334" target="_blank" >RIV/60461373:22340/25:43933334 - isvavai.cz</a>

  • Result on the web

    <a href="https://onlinelibrary.wiley.com/doi/full/10.1002/pro.70047" target="_blank" >https://onlinelibrary.wiley.com/doi/full/10.1002/pro.70047</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/pro.70047" target="_blank" >10.1002/pro.70047</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Exploring the proton transport mechanism of the mitochondrial ADP/ATP carrier: FA-cycling hypothesis and beyond

  • Original language description

    The mitochondrial ADP/ATP carrier (AAC, ANT), a member of the SLC25 family of solute carriers, plays a critical role in transporting purine nucleotides (ATP and ADP) as well as protons across the inner mitochondrial membrane. However, the precise mechanism and physiological significance of proton transport by ADP/ATP carrier remain unclear. Notably, the presence of uncouplers—such as long-chain fatty acids (FA) or artificial compounds like dinitrophenol (DNP)—is essential for this process. We explore two potential mechanisms that describe ADP/ATP carrier as either (i) a proton carrier that functions in the presence of FA or DNP, or (ii) an anion transporter (FA− or DNP). In the latter case, the proton is translocated by the neutral form of FA, which carries it from the matrix to the intermembrane space (FA-cycling hypothesis). Our recent results support this hypothesis. We describe a four-step mechanism for the “sliding” of the FA anion from the matrix to the mitochondrial intermembrane space and discuss a possible generalization of this mechanism to other SLC25 carriers. © 2025 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>SC</sub> - Article in a specialist periodical, which is included in the SCOPUS database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    PROTEIN SCIENCE

  • ISSN

    0961-8368

  • e-ISSN

    1469-896X

  • Volume of the periodical

    34

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    "January"

  • UT code for WoS article

  • EID of the result in the Scopus database

    2-s2.0-85218260480