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Related Concept Videos

¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

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This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
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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.
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When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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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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Related Experiment Video

Updated: Apr 30, 2026

Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies
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PQQ-dependent methanol dehydrogenases: rare-earth elements make a difference.

Jan T Keltjens1, Arjan Pol, Joachim Reimann

  • 1Department of Microbiology, Institute of Wetland and Water Research, Radboud University Nijmegen, Heyendaalseweg 135, 6525AJ, Nijmegen, The Netherlands.

Applied Microbiology and Biotechnology
|May 13, 2014
PubMed
Summary

New methanol dehydrogenase (MDH) enzymes, XoxF-MDHs, utilize rare-earth elements for enhanced efficiency in methanol oxidation. These enzymes differ from previously studied MxaFI-MDHs, opening new metabolic possibilities.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Methanol dehydrogenase (MDH) is crucial for methanol metabolism in methylotrophic and methanotrophic bacteria.
  • Gram-negative bacteria utilize pyrroloquinoline quinone (PQQ)-dependent MDHs, including the heterotetrameric MxaFI-MDH, which uses calcium as a cofactor.
  • Genomic data suggested the existence of a distinct MDH family, now identified as XoxF-MDHs.

Purpose of the Study:

  • To characterize the novel XoxF-MDHs and compare their structure and function to the well-studied MxaFI-MDHs.
  • To investigate the role of rare-earth elements (REEs) as cofactors in XoxF-MDH catalysis.
  • To explore the metabolic implications and evolutionary significance of XoxF-MDHs.

Main Methods:

  • Isolation and characterization of XoxF-MDH enzymes.
  • Structural analysis comparing MxaFI-MDH and XoxF-MDH.
  • Bioinformatic and genomic analyses to assess the prevalence of XoxF-MDHs and related REE-containing quinoproteins.

Main Results:

  • XoxF-MDHs are homodimeric proteins that lack the small subunit found in MxaFI-MDHs.
  • XoxF-MDHs employ rare-earth elements (e.g., lanthanides) instead of calcium, potentially enhancing catalytic efficiency.
  • XoxF-MDHs oxidize methanol to formate, unlike MxaFI-MDHs which produce formaldehyde.
  • A specific aspartate residue is crucial for REE binding in XoxF-MDHs.
  • XoxF-MDHs and other REE-containing quinoproteins are widespread in microbial genomes, indicating significant, yet unexploited, metabolic potential.

Conclusions:

  • XoxF-MDHs represent a distinct class of MDHs with unique cofactor requirements and catalytic outcomes.
  • The use of REEs in XoxF-MDHs suggests novel biochemical pathways and potential for biotechnological applications.
  • The broad distribution of XoxF-MDHs highlights their importance in microbial metabolism and the underappreciated role of REE-dependent enzymes.