Mechanistic Interrogation of a PQQ and Rare Earth-Dependent Artificial Metalloenzyme

Mechanistic Interrogation of a PQQ and Rare Earth-Dependent Artificial Metalloenzyme

Pyrroloquinoline quinone (PQQ)-binding proteins are found in diverse species and play key roles in the central metabolism of many methylotrophic bacteria, acting as redox-active cofactors in their alcohol dehydrogenase (ADH) enzymes. These enzymes also require a Lewis acidic metal ion to activate PQ...

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Bibliographic Details
Main Author: Mohd Taher (22385539) (author)
Other Authors: Peter J. Thompson (13921641) (author), Carlos Nava-Matadamas (22385542) (author), Austin T. Bruchs (22385545) (author), Jennifer Bridwell-Rabb (1329231) (author), Lisa Olshansky (1343817) (author)
Published: 2025
Subjects:
Biophysics
Biochemistry
Physiology
Infectious Diseases
Computational Biology
Chemical Sciences not elsewhere classified
play key roles
molecular dynamics simulations
many methylotrophic bacteria
increasing lewis acidity
electron transport processes
conformational dynamics associated
9 ± 0
studies provide insights
observed decreasing reactivity
metal ions spanning
rare earth series
kinetic isotope effect
enzymes also require
natural adh assays
biomimetic active site
rare earth
patterns observed
natural mdhs
metal ion
computational studies
active cofactors
report mechanistic
relative reactivities
ray diffraction
preparing arms
pattern consistent
mechanistic interrogation
functional properties
diverse species
dependent enzymes
central metabolism
artificial metalloenzyme
alcohol dehydrogenase
2011 discovery
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