Interaction of Flavonoids with Zinc and Zinc-Containing Enzymes

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00558561" target="_blank" >RIV/61388971:_____/22:00558561 - isvavai.cz</a>

Alternative codes found

RIV/60076658:12310/22:43904988 RIV/00216208:11160/22:10450280

Result on the web

<a href="https://pubs.acs.org/doi/10.1021/acs.jafc.2c01446" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.jafc.2c01446</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.jafc.2c01446" target="_blank" >10.1021/acs.jafc.2c01446</a>

Result language

angličtina

Original language name

Interaction of Flavonoids with Zinc and Zinc-Containing Enzymes

Original language description

The current chelation therapy has several drawbacks, including lack of selectivity, which could lead to trace metal depletion. Consequently, the proper function of metalloenzymes can be disrupted. Flavonoids possess chelating properties and hence interfere with the homeostasis of essential metals. We focused on zinc, an important trace metal required for the function of many enzymes and transcription factors. After making an initial evaluation of the Zn2+-chelating properties of a series of flavonoids, the effect of these compounds on various zinc-containing enzymes was also investigated. We performed enzyme inhibition assays spectrophotometrically using yeast and equine alcohol dehydrogenases and bovine glutamate dehydrogenase. Nine of the 21 flavonoids tested were capable of chelating Zn2+. Baicalein and 3-hydroxyflavone were the most potent Zn2+ chelators under slightly acidic and neutral pH conditions. This chelation was also confirmed by the ability to reverse Zn2+-induced enzymatic inhibition of bovine glutamate dehydrogenase. Although some flavonoids were also able to inhibit zinc-containing alcohol dehydrogenases, this inhibition was likely not caused by Zn2+ chelation. Luteolin was a relatively potent inhibitor of these enzymes regardless of the presence of Zn2+. Docking studies confirmed the binding of active flavonoids to equine alcohol dehydrogenase without any significant interaction with the catalytic zinc.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/EF19_073%2F0016935" target="_blank" >EF19_073/0016935: Grant schemes at Charles University</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2022

Confidentiality

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

Name of the periodical

Journal of Agricultural and Food Chemistry

ISSN

0021-8561

e-ISSN

1520-5118

Volume of the periodical

70

Issue of the periodical within the volume

20

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

6134-6144

UT code for WoS article

000805989400017

EID of the result in the Scopus database

2-s2.0-85130735986