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Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site.
- Source :
-
The FEBS journal [FEBS J] 2023 Jun; Vol. 290 (11), pp. 2939-2953. Date of Electronic Publication: 2023 Jan 19. - Publication Year :
- 2023
-
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.<br /> (© 2023 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Details
- Language :
- English
- ISSN :
- 1742-4658
- Volume :
- 290
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- The FEBS journal
- Publication Type :
- Academic Journal
- Accession number :
- 36617384
- Full Text :
- https://doi.org/10.1111/febs.16722