Metal ion's central role in PQQ-dependent alcohol dehydrogenases
Abstract
In the past fifteen years, there has been an outbreak in the research on lanthanide (Ln) biochemistry due to the discovery of Ln-using bacteria in 2011, and the identification of the first and only known family of Ln-dependent enzymes, namely Lndependent alcohol dehydrogenases (Ln-ADH). These enzymes are closely related to Ca-dependent alcohol dehydrogenases (Ca-ADH), although the two enzyme families are encoded by different genes. Ln 3+ tune Ln-ADH reactivity to an extent that was unexpected. The enzyme is highly active with the early less Lewis acidic Ln 3+ , and inactive with the late Ln 3+ . Several studies have tried to understand this contrasted reactivity, either by looking directly at the enzyme or by designing enzyme mimics, and by combining both experimental evidences and computational modeling. Despite these efforts, a clear understanding of the role of the metal ion (Ca 2+ , Ln 3+ ) in the catalysis is still lacking. This review provides an overview of the actual knowledge on the reactivity of Ln-ADH and the closely related Ca-ADH. In light of these data, it critically presents and discusses the actual hypotheses proposed to explain the central role of the metal ion in the catalysis.
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BibTeX
@article{zimmeter2026metal,
title = {{Metal ion's central role in PQQ-dependent alcohol dehydrogenases}},
author = {Katharina Zimmeter and Alicia Voge and Christelle Hureau and Emilie Mathieu},
journal = {Dalton Transactions},
year = {2026},
month = oct,
doi = {10.1039/d6dt01826b},
url = {https://hal.science/hal-05836579v1},
note = {CC BY-NC 4.0},
}
RIS
TY - JOUR
TI - Metal ion's central role in PQQ-dependent alcohol dehydrogenases
AU - Katharina Zimmeter
AU - Alicia Voge
AU - Christelle Hureau
AU - Emilie Mathieu
PY - 2026
DA - 2026/10/16
JO - Dalton Transactions
DO - 10.1039/d6dt01826b
UR - https://hal.science/hal-05836579v1
AB - In the past fifteen years, there has been an outbreak in the research on lanthanide (Ln) biochemistry due to the discovery of Ln-using bacteria in 2011, and the identification of the first and only known family of Ln-dependent enzymes, namely Lndependent alcohol dehydrogenases (Ln-ADH). These enzymes are closely related to Ca-dependent alcohol dehydrogenases (Ca-ADH), although the two enzyme families are encoded by different genes. Ln 3+ tune Ln-ADH reactivity to an extent that was unexpected. The enzyme is highly active with the early less Lewis acidic Ln 3+ , and inactive with the late Ln 3+ . Several studies have tried to understand this contrasted reactivity, either by looking directly at the enzyme or by designing enzyme mimics, and by combining both experimental evidences and computational modeling. Despite these efforts, a clear understanding of the role of the metal ion (Ca 2+ , Ln 3+ ) in the catalysis is still lacking. This review provides an overview of the actual knowledge on the reactivity of Ln-ADH and the closely related Ca-ADH. In light of these data, it critically presents and discusses the actual hypotheses proposed to explain the central role of the metal ion in the catalysis.
SN - 1477-9226
SN - 1477-9234
ER -