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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would...
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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction...
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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
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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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Biphasic Proton Transport Mechanism for Uncoupling Proteins.

Afshan Ardalan1, Shahin Sowlati-Hashjin2,3, Habib Oduwoye1

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Uncoupling proteins (UCPs) transport protons through conformational changes. This study reveals UCP2

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Membrane Protein Function

Background:

  • Uncoupling proteins (UCPs) mediate proton transport across membranes via conformational state changes.
  • Salt-bridge networks in UCPs are critical for regulating these cytoplasmic and matrix states.
  • Understanding UCP2's mechanism is key to elucidating its role in cellular energy regulation.

Purpose of the Study:

  • To investigate the role of the matrix salt-bridge network in UCP2 proton transport.
  • To elucidate the structural and functional mechanisms of proton transport in tetrameric UCP2.
  • To propose a molecular model for UCP2 proton transport and its regulation.

Main Methods:

  • Site-directed mutagenesis to create UCP2 mutants targeting matrix salt-bridges.
  • Recombinant protein expression in E. coli membranes and reconstitution into lipid bilayers.
  • Analysis using gel electrophoresis, circular dichroism, fluorescence assays, and molecular dynamics simulations.

Main Results:

  • Identified five salt-bridges in the UCP2 matrix network, more than previously reported.
  • Demonstrated that the matrix network regulates proton transport by stabilizing helix proximity and limiting activator binding.
  • Proposed a biphasic two-state model for proton transport in functional tetrameric UCP2.
  • Showed ATP inhibits UCP2 by occluding the pore via interactions with matrix network residues.

Conclusions:

  • The UCP2 matrix network is crucial for regulating proton transport and conformational state transitions.
  • A detailed molecular model for UCP2 proton transport and purine nucleotide inhibition is proposed.
  • Findings provide novel insights into the complex mechanism of UCP-mediated proton transport.