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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Electron Transport Chain: Complex I and II01:46

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Electron Transport Chain: Complex III and IV01:43

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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 Supercomplexes in the Crista Membrane01:41

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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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tRNA Activation02:26

tRNA Activation

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Structure of the ATP-driven methyl-coenzyme M reductase activation complex.

Fidel Ramírez-Amador1,2, Sophia Paul1,2, Anuj Kumar1,2

  • 1Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, Marburg, Germany.

Nature
|April 16, 2025
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Summary

Researchers elucidated the activation mechanism of Methyl-coenzyme M reductase (MCR), the key enzyme for methane production. They discovered an ATP-dependent activation complex containing iron-sulfur clusters, shedding light on ancient bioenergetic processes.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Methyl-coenzyme M reductase (MCR) catalyzes methane formation, a vital biological process.
  • The active site cofactor, coenzyme F430, requires nickel in the Ni(I) state for activity.
  • The reductive activation mechanism of F430 within MCR is poorly understood.

Purpose of the Study:

  • To investigate the mechanism of MCR activation in methanogenic archaea.
  • To characterize the MCR activation complex and its components.
  • To elucidate the structural basis of F430 reductive activation.

Main Methods:

  • Purification and characterization of the MCR activation complex from Methanococcus maripaludis.
  • In vitro functional assays demonstrating ATP-dependent MCR activation.
  • Cryo-electron microscopy (cryo-EM) for structural determination.
  • Topology and electron paramagnetic resonance (EPR) spectroscopy.

Main Results:

  • Identified an MCR activation complex involving McrC and other proteins.
  • Demonstrated strict ATP dependence for MCR activation in vitro.
  • Determined cryo-EM structures of the complex at high resolution (1.8-2.1 Å).
  • Revealed three complex iron-sulfur clusters forming an electron transfer pathway to F430.

Conclusions:

  • The MCR activation complex facilitates the reductive activation of F430.
  • The identified iron-sulfur clusters resemble nitrogenase maturation intermediates, suggesting evolutionary links.
  • Provides mechanistic insights into MCR function and the evolution of ancient enzymes.