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- W4313784154 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." @default.
- W4313784154 created "2023-01-08" @default.
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- W4313784154 date "2023-01-19" @default.
- W4313784154 modified "2023-09-25" @default.
- W4313784154 title "Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase <scp>CntA</scp> catalytic site" @default.
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- W4313784154 doi "https://doi.org/10.1111/febs.16722" @default.
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