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TitleStructural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase.
Journal, issue, pagesNat Chem, Year 2024
Publish dateMay 14, 2024
AuthorsBasavraj Khanppnavar / Joel P S Choo / Peter-Leon Hagedoorn / Grigory Smolentsev / Saša Štefanić / Selvapravin Kumaran / Dirk Tischler / Fritz K Winkler / Volodymyr M Korkhov / Zhi Li / Richard A Kammerer / Xiaodan Li /
PubMed AbstractMembrane-bound styrene oxide isomerase (SOI) catalyses the Meinwald rearrangement-a Lewis-acid-catalysed isomerization of an epoxide to a carbonyl compound-and has been used in single and cascade ...Membrane-bound styrene oxide isomerase (SOI) catalyses the Meinwald rearrangement-a Lewis-acid-catalysed isomerization of an epoxide to a carbonyl compound-and has been used in single and cascade reactions. However, the structural information that explains its reaction mechanism has remained elusive. Here we determine cryo-electron microscopy (cryo-EM) structures of SOI bound to a single-domain antibody with and without the competitive inhibitor benzylamine, and elucidate the catalytic mechanism using electron paramagnetic resonance spectroscopy, functional assays, biophysical methods and docking experiments. We find ferric haem b bound at the subunit interface of the trimeric enzyme through H58, where Fe(III) acts as the Lewis acid by binding to the epoxide oxygen. Y103 and N64 and a hydrophobic pocket binding the oxygen of the epoxide and the aryl group, respectively, position substrates in a manner that explains the high regio-selectivity and stereo-specificity of SOI. Our findings can support extending the range of epoxide substrates and be used to potentially repurpose SOI for the catalysis of new-to-nature Fe-based chemical reactions.
External linksNat Chem / PubMed:38744914
MethodsEM (single particle)
Resolution2.048 - 2.12 Å
Structure data

17785

8pnu

EMDB-17785, PDB-8pnu:
Cryo-EM structure of styrene oxide isomerase bound to benzylamine inhibitor
Method: EM (single particle) / Resolution: 2.12 Å

17786

8pnv

EMDB-17786, PDB-8pnv:
Cryo-EM structure of styrene oxide isomerase
Method: EM (single particle) / Resolution: 2.048 Å

Chemicals

ChemComp-ABN:
BENZYLAMINE / Benzylamine

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-HOH:
WATER / Water

Source
  • pseudomonas sp. vlb120 (bacteria)
  • vicugna pacos (alpaca)
KeywordsMEMBRANE PROTEIN / Heme binding protein / Enzyme / Isomerase

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