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首页> 外文期刊>The FEBS journal. >Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site
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Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site

机译：Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site

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摘要

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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