Mutations of methionine 444 interacting with T1Cu-coordinating amino acids affect the structure and function of multicopper oxidase CopA.
Manganese oxidizing bacteria
Manganese removal
Multicopper oxidase
Site-directed mutagenesis
Journal
Biodegradation
ISSN: 1572-9729
Titre abrégé: Biodegradation
Pays: Netherlands
ID NLM: 9100834
Informations de publication
Date de publication:
29 Oct 2024
29 Oct 2024
Historique:
received:
09
06
2024
accepted:
16
09
2024
medline:
29
10
2024
pubmed:
29
10
2024
entrez:
29
10
2024
Statut:
epublish
Résumé
Manganese is an essential trace element for humans, animals, and plants, but excessive amounts of manganese can cause serious harm to organisms. The biological manganese oxidation process mainly oxidizes Mn(II) through the secretion of unique manganese oxidase by manganese-oxidizing bacteria. The T1 Cu site of multicopper oxidase is the main site for substrate oxidation, and its role is to transfer electrons to TNC, where dioxygen reduction occurs. In this study, methionine (Met) No. 444 interacting with the T1Cu-coordinating amino acid in the multicopper oxidase CopA from Brevibacillus panacihumi MK-8 was mutated to phenylalanine (Phe) and leucine (Leu) by the enzyme. Based on the analysis of enzymatic properties and the structural model, the mutant protein M444F with 4.58 times the catalytic efficiency of the original protein CopA and the mutant protein M444L with 1.67 times the catalytic efficiency of the original protein CopA were obtained. The study showed that the manganese removal rate of the manganese-oxidizing engineered bacterium Rosetta-pET-copA
Identifiants
pubmed: 39470852
doi: 10.1007/s10532-024-10102-4
pii: 10.1007/s10532-024-10102-4
doi:
Substances chimiques
Methionine
AE28F7PNPL
Bacterial Proteins
0
Manganese
42Z2K6ZL8P
Copper
789U1901C5
Oxidoreductases
EC 1.-
CopA protein, Bacteria
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2Subventions
Organisme : National Natural Science Foundation of China
ID : 22176146
Organisme : Science and Technology Commission of Shanghai Municipality
ID : 19ZR1459400
Organisme : China Scholarship Council
ID : 201706265024
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer Nature B.V.
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