Catalytic artificial nitroalkane oxidases - a way towards organocatalytic umpolung

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22310%2F23%3A43926305" target="_blank" >RIV/60461373:22310/23:43926305 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22810/23:43926305

Výsledek na webu

<a href="https://pubs.rsc.org/en/content/articlepdf/2023/ob/d3ob00101f" target="_blank" >https://pubs.rsc.org/en/content/articlepdf/2023/ob/d3ob00101f</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/d3ob00101f" target="_blank" >10.1039/d3ob00101f</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Catalytic artificial nitroalkane oxidases - a way towards organocatalytic umpolung

Popis výsledku v původním jazyce

Nitroalkane oxidases (NAOs) are flavoenzymes that catalyse the oxidation of nitroalkanes to their corresponding carbonyl compounds while producing nitrite anions. Herein, we present an artificial catalytic system using flavins or ethylene-bridged flavinium salts that works via an NAO-like process. Under conditions optimised in terms of solvent, base, temperature and oxygen pressure, primary nitroalkanes were transformed to aldehydes. In our system, aldehydes immediately reacted with other nitroalkane molecules to form β-nitroalcohols. The reduced flavin catalyst was re-oxidised by oxygen. An alternative mechanism towards β-nitroalcohols via 5-(2-nitrobutyl)-1,5-dihydroflavin was suggested through quantum chemical calculations and by trapping and characterising this dihydroflavin intermediate. Interestingly, 5-(2-nitrobutyl)-1,5-dihydroflavin is an analogue of the flavin adenine dinucleotide adduct previously observed in an NAO X-ray structure. In both mechanistic pathways, flavin-5-iminium species is formed by nitroalkanide addition to flavin. This process represents flavin-based umpolung of an original donor to an acceptor. © 2023 The Royal Society of Chemistry.

Název v anglickém jazyce

Catalytic artificial nitroalkane oxidases - a way towards organocatalytic umpolung

Popis výsledku anglicky

Nitroalkane oxidases (NAOs) are flavoenzymes that catalyse the oxidation of nitroalkanes to their corresponding carbonyl compounds while producing nitrite anions. Herein, we present an artificial catalytic system using flavins or ethylene-bridged flavinium salts that works via an NAO-like process. Under conditions optimised in terms of solvent, base, temperature and oxygen pressure, primary nitroalkanes were transformed to aldehydes. In our system, aldehydes immediately reacted with other nitroalkane molecules to form β-nitroalcohols. The reduced flavin catalyst was re-oxidised by oxygen. An alternative mechanism towards β-nitroalcohols via 5-(2-nitrobutyl)-1,5-dihydroflavin was suggested through quantum chemical calculations and by trapping and characterising this dihydroflavin intermediate. Interestingly, 5-(2-nitrobutyl)-1,5-dihydroflavin is an analogue of the flavin adenine dinucleotide adduct previously observed in an NAO X-ray structure. In both mechanistic pathways, flavin-5-iminium species is formed by nitroalkanide addition to flavin. This process represents flavin-based umpolung of an original donor to an acceptor. © 2023 The Royal Society of Chemistry.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10401 - Organic chemistry

Projekt

<a href="/cs/project/GA21-14179S" target="_blank" >GA21-14179S: Nová strategie přepólování s využitím kovalentní organokatalýzy s flaviny</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Organic and Biomolecular Chemistry

ISSN

1477-0520

e-ISSN

—

Svazek periodika

21

Číslo periodika v rámci svazku

13

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

2768-2774

Kód UT WoS článku

000949783200001

EID výsledku v databázi Scopus

2-s2.0-85151003177