Structural and functional characterization of dihydrodiol dehydrogenase PahB recognizing high-molecular-weight PAH substrates
Qun Han, Lin-Lin Tian, Lu Guo, Rui Cui, Ze-Shen Liu, De-Feng Li · 2026
Read Structural and functional characterization of dihydrodiol dehydrogenase PahB recognizing high-molecular-weight PAH substrates by Qun Han, Lin-Lin Tian, Lu Guo, Rui Cui, Ze-Shen Liu, De-Feng Li (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13390466.txt.
Description
Qun Han and colleagues characterise, in 2026, an enzyme that helps a bacterium break down some of the most stubborn oil-related pollutants in soil and water. Large polycyclic aromatic hydrocarbons resist removal, yet the strain Altererythrobacter species H2 can degrade several of them, including benzo[a]pyrene.
Breakdown starts with well-studied oxygen-adding enzymes, but the next dehydrogenation step is less understood. The team examined that step's enzyme, PahB, mapping which breakdown products it can oxidise and how it recognises them. Environmental microbiologists gain structural and family-tree detail on a bottleneck enzyme, knowledge that can guide the design of cleanup strains for heavy hydrocarbon pollution.
Catalog record
| CREATOR | Qun Han, Lin-Lin Tian, Lu Guo, Rui Cui, Ze-Shen Liu, De-Feng Li |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 41642 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |