Local Charge Distributions, Electric Dipole Moments, and Local Electric Fields Influence Reactivity Patterns and Guide Regioselectivities in α-Ketoglutarate-Dependent Non-heme Iron Dioxygenases

Autor: Hatem Salama Ali, Gourab Mukherjee, Hafiz Saqib Ali, Sam De Visser

Publikováno v: Accounts of Chemical Research. 55:65-74

Non-heme iron dioxygenases catalyze vital processes for human health related to the biosynthesis of essential products and the biodegradation of toxic metabolites. Often the natural product biosyntheses by these non-heme iron dioxygenases is highly r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f96520b58e329a46848c6af7e815fd5e
https://doi.org/10.1021/acs.accounts.1c00538

Density Functional Theory Study into the Reaction Mechanism of Isonitrile Biosynthesis by the Nonheme Iron Enzyme ScoE

Autor: Sidra Ghafoor, Hatem Salama Ali, Hafiz Saqib Ali, Sam De Visser

Publikováno v: Topics in Catalysis. 65:528-543

The nonheme iron enzyme ScoE catalyzes the biosynthesis of an isonitrile substituent in a peptide chain. To understand details of the reaction mechanism we created a large active site cluster model of 212 atoms that contains substrate, the active oxi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bced506fdb1d157c14f40b7e083000e1
https://doi.org/10.1007/s11244-021-01460-x

Lignin Biodegradation by a Cytochrome P450 Enzyme: A Computational Study into Syringol Activation by GcoA

Autor: Hatem Salama Ali, Richard Henchman, Hafiz Saqib Ali, Sam De Visser

Publikováno v: Ali, H S, Henchman, R & De Visser, S 2020, ' Lignin biodegradation by a cytochrome P450 enzyme: A computational study into syringol activation by GcoA ', Chemistry – A European Journal . https://doi.org/10.1002/chem.202002203
Chemistry (Weinheim an Der Bergstrasse, Germany)

A recently characterized cytochrome P450 isozyme GcoA activates lignin components through a selective O‐demethylation or alternatively an acetal formation reaction. These are important reactions in biotechnology and, because lignin is readily avail

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b2ec980360879beadb541e0ece0e840
https://doi.org/10.1002/chem.202002203

Electrostatic Perturbations in the Substrate‐Binding Pocket of Taurine/α‐Ketoglutarate Dioxygenase Determine its Selectivity

Autor: Hatem Salama Ali, Hafiz Saqib Ali, Sam De Visser

Publikováno v: Ali, H S & De Visser, S 2021, ' Electrostatic perturbations in the substrate-binding pocket of taurine/α-ketoglutarate dioxygenase determine its selectivity ', Chemistry – A European Journal . https://doi.org/10.1002/chem.202104167

Taurine/α-ketoglutarate dioxygenase is an important enzyme that takes part in the cysteine catabolism process in the human body and selectively hydroxylates taurine at the C¹-position. Recent computational studies showed that in the gas-phase the C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d23fc508f6363e4d6e0f5c882a0d7aac
https://doi.org/10.1002/chem.202104167

Electrostatic Perturbations from the Protein Affect C-H Bond Strengths of the Substrate and Enable Negative Catalysis in the TmpA Biosynthesis Enzyme

Autor: Hatem Salama Ali, Hafiz Saqib Ali, YEN-TING LIN, Sam De Visser

Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany). 27(34)

The nonheme iron dioxygenase 2-(trimethylammonio)-ethylphosphonate dioxygenase (TmpA) is an enzyme involved in the regio- and chemoselective hydroxylation at the C 1 -position of the substrate as part of the biosynthesis of glycine betaine in bacteri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a886842bc19d3a42ff0588943c79ef1
https://pubmed.ncbi.nlm.nih.gov/33978257