Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site.
FEBS J
; 290(11): 2939-2953, 2023 06.
Article
em En
| MEDLINE
| ID: mdl-36617384
ABSTRACT
Rieske monooxygenases undertake complex catalysis integral to marine, terrestrial and human gut-ecosystems. Group-I to -IV Rieske monooxygenases accept aromatic substrates and have well-characterised catalytic mechanisms. Nascent to our understanding are Group-V members catalysing the oxidation/breakdown of quaternary ammonium substrates. Phylogenetic analysis of Group V highlights a cysteine residue-pair adjacent to the mononuclear Fe active site with no established role. Following our elucidation of the carnitine monooxygenase CntA structure, we probed the function of the cysteine pair Cys206/Cys209. Utilising biochemical and biophysical techniques, we found the cysteine residues do not play a structural role nor influence the electron transfer pathway, but rather are used in a nonstoichiometric role to ensure the catalytic iron centre remains in an Fe(II) state.
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Texto completo:
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cisteína
/
Oxigenases de Função Mista
Limite:
Humans
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article