Impact of the T296S mutation in P450 GcoA for aryl-O-demethylation: a QM/MM study
Sonia F. G. Santos, Rajesh Reddy Bommareddy, Gary W. Black, Warispreet Singh · 2024
Read Impact of the T296S mutation in P450 GcoA for aryl-O-demethylation: a QM/MM study by Sonia F. G. Santos, Rajesh Reddy Bommareddy, Gary W. Black, Warispreet Singh (2024) 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/pmc-10811788.txt.
Description
Lignin, the tough polymer in plant walls, could become a renewable source of valuable aromatic chemicals. One step on that path is an enzyme that strips a methyl group from p-vanillin, and a single mutation, T296S, lets the enzyme do it. Sonia Santos and co-authors use quantum and molecular simulations to learn why the change works.
The calculations show the mutated enzyme lets p-vanillin flex into a pose that places its methoxy group right beside the reactive iron-oxygen center. Pulling off a hydrogen atom emerges as the slow step, matching experiments. The detailed geometry of the reaction path helps explain the gain and may guide further enzyme tuning for green chemistry.
Catalog record
| CREATOR | Sonia F. G. Santos, Rajesh Reddy Bommareddy, Gary W. Black, Warispreet Singh |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 23 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |