How Can Methanol Dehydrogenase from Methylacidiphilum fumariolicum Work with the Alien CeIII Ion in the Active Center? A Theoretical Study.

@article{Prejan2017HowCM,
  title={How Can Methanol Dehydrogenase from Methylacidiphilum fumariolicum Work with the Alien CeIII Ion in the Active Center? A Theoretical Study.},
  author={Mario Prejan{\`o} and T. Marino and N. Russo},
  journal={Chemistry},
  year={2017},
  volume={23 36},
  pages={
          8652-8657
        }
}
  • Mario Prejanò, T. Marino, N. Russo
  • Published 2017
  • Medicine, Chemistry
  • Chemistry
    • Lanthanides are an example of nonbiogenic metal species and have been widely used in crystallographic and spectroscopic studies to probe Mg2+ /Ca2+ binding sites in metalloproteins by replacing the native cofactor. Recently, a methanol dehydrogenase (MDH) enzyme containing cerium ion in the active site has been isolated from Methylacidiphilum fumariolicum bacterium. With the aim to highlight as metal ion substitution can be reflected in catalytic mechanism, a comparative DFT study between Ca… CONTINUE READING
    View on PubMed
    doi.org
    25 Citations
    Background Citations
    2
    Methods Citations
    2
    25 Citations
    Citation Type

    Citation Type

    How the lanthanide ions affect the addition-elimination step of methanol dehydrogenases.
    • 2
    How Metal Coordination in the Ca-, Ce-, and Eu-Containing Methanol Dehydrogenase Enzymes Can Influence the Catalysis: A Theoretical Point of View
    • 3
    Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function
    • 6
    Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and function
    • PDF
    Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
    • 29
    Role of rare earth elements in methanol oxidation.
    • 25
    Biochemical and Structural Characterization of XoxG and XoxJ and Their Roles in Lanthanide‐Dependent Methanol Dehydrogenase Activity
    • 13
    Functional Synthetic Model for the Lanthanide-Dependent Quinoid Alcohol Dehydrogenase Active Site.
    • 19
    Why hydroxy-proline improves the catalytic power of the peptidoglycan N-deacetylase enzyme: insight from theory.
    • 2
    Electrocatalysis of a Europium-Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron-Acceptor Cytochrome cGJ.
    • 5

    References

    SHOWING 1-10 OF 47 REFERENCES
    DFT study of the active site of the XoxF-type natural, cerium-dependent methanol dehydrogenase enzyme.
    • 43
    Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation.
    • 57
    • PDF
    The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.
    • 174
    • PDF
    Kinetic and spectral studies on the redox forms of methanol dehydrogenase from Hyphomicrobium X.
    • 59
    Methanol dehydrogenase, a PQQ-containing quinoprotein dehydrogenase.
    • C. Anthony
    • Chemistry, Medicine
    • Sub-cellular biochemistry
    • 2000
    • 65
    Catalytic activity of a ζ-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms.
    • 37
    Catalytic mechanism of the arylsulfatase promiscuous enzyme from Pseudomonas aeruginosa.
    • 40
    Quantum chemical modeling of methanol oxidation mechanisms by methanol dehydrogenase enzyme: effect of substitution of calcium by barium in the active site.
    • 16
    Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase
    • 25
    • PDF
    Reaction mechanism of the binuclear zinc enzyme glyoxalase II - A theoretical study.
    • 31