Moco Carrier and Binding Proteins.


Journal

Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009

Informations de publication

Date de publication:
04 Oct 2022
Historique:
received: 31 08 2022
revised: 25 09 2022
accepted: 26 09 2022
entrez: 14 10 2022
pubmed: 15 10 2022
medline: 18 10 2022
Statut: epublish

Résumé

The molybdenum cofactor (Moco) is the active site prosthetic group found in numerous vitally important enzymes (Mo-enzymes), which predominantly catalyze 2 electron transfer reactions. Moco is synthesized by an evolutionary old and highly conserved multi-step pathway, whereby the metal insertion reaction is the ultimate reaction step here. Moco and its intermediates are highly sensitive towards oxidative damage and considering this, they are believed to be permanently protein bound during synthesis and also after Moco maturation. In plants, a cellular Moco transfer and storage system was identified, which comprises proteins that are capable of Moco binding and release but do not possess a Moco-dependent enzymatic activity. The first protein described that exhibited these properties was the Moco carrier protein (MCP) from the green alga

Identifiants

pubmed: 36235107
pii: molecules27196571
doi: 10.3390/molecules27196571
pmc: PMC9571131
pii:
doi:

Substances chimiques

Carrier Proteins 0
Coenzymes 0
Metalloproteins 0
Molybdenum Cofactors 0
Molybdenum 81AH48963U

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Deutsche Forschungsgemeinschaft
ID : GRK 2223/1

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Auteurs

Tobias Kruse (T)

Institute of Plant Biology, Technische Universität Braunschweig, 38106 Braunschweig, Germany.

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Classifications MeSH