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Related Concept Videos

The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
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Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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ATP and Energy Production01:23

ATP and Energy Production

2.4K
Adenosine triphosphate (ATP) is a critical molecule that functions as the main energy carrier in cells. Structurally, ATP consists of an adenosine molecule—comprising adenine and ribose—bonded to three phosphate groups. The high-energy bonds between these phosphate groups store significant amounts of potential energy. This energy is released during hydrolysis, wherein ATP is converted to adenosine diphosphate (ADP) or adenosine monophosphate (AMP), driving a variety of essential...
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Dataset of the AAC2 conformations in the c-, intermediate- and m-states obtained from free-energy simulations.

Data in brief·2016
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The switching mechanism of the mitochondrial ADP/ATP carrier explored by free-energy landscapes.

Biochimica et biophysica acta·2016
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Wanderings in bioenergetics and biomembranes.

Biochimica et biophysica acta·2010
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Cardiolipin and mitochondrial carriers.

Biochimica et biophysica acta·2009
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The ADP and ATP transport in mitochondria and its carrier.

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Transport viewed as a catalytic process.

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Related Experiment Video

Updated: Mar 12, 2026

A Micro-agar Salt Bridge Electrode for Analyzing the Proton Turnover Rate of Recombinant Membrane Proteins
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A Micro-agar Salt Bridge Electrode for Analyzing the Proton Turnover Rate of Recombinant Membrane Proteins

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UCP1 - A sophisticated energy valve.

Martin Klingenberg1

  • 1Institut für physiologische Chemie, Universität München, Schillerstr. 44, 80336 München, Germany.

Biochimie
|October 31, 2016
PubMed
Summary

Uncoupling protein 1 (UCP1) facilitates proton transport, acting as a key thermogenic factor. Research reveals fatty acids

Area of Science:

  • Biochemistry and Molecular Biology
  • Mitochondrial Physiology
  • Thermogenesis Research

Background:

  • The review traces the biochemical investigation of Uncoupling Protein 1 (UCP1) from its initial discovery.
  • Early work involved isolating native UCP1 and determining its amino acid sequence, revealing homology to the ADP/ATP carrier.
  • Focus on UCP1's structural and functional characteristics, particularly its complex nucleotide binding properties.

Observation:

  • Nucleotide binding to UCP1 exhibits significant pH dependence, with distinct interactions for diphospho- and triphosphonucleotides.
  • Identification of specific residues controlling nucleotide binding site access via H+ dissociation.
  • Fluorescent nucleotide derivatives revealed a two-state nucleotide binding model (loose and tight UCP1 conformations) impacting H+ transport inhibition, characterized by slow transitions between states.
Keywords:
Brown adipose tissueFatty acidH(+) transportMitochondriaUncoupling proteinUncoupling regulation

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Findings:

  • Reconstitution of isolated UCP1 into vesicles confirmed its role as the primary uncoupling factor, not merely a nucleotide-regulated channel.
  • Proton (H+) transport by UCP1 is electrophoretic and linearly related to membrane potential.
  • Characterization of fatty acid (FA) dependence on H+ transport, addressing discrepancies across research groups and proposing indirect mechanisms for FA to alleviate nucleotide inhibition in mitochondria, including pH shifts and cardiolipin interactions.

Implications:

  • A revised model for FA-mediated H+ transport in UCP1 is proposed, where FA acts as an immobile prosthetic group within the translocation channel.
  • This mechanism involves alternating gate openings to facilitate H+ uptake and release, modulating mitochondrial function.
  • Understanding UCP1's intricate regulation by nucleotides and fatty acids is crucial for unraveling its role in energy metabolism and thermogenesis.