Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site

Artificial maturation of hydrogenases provides a path towards generating new semi-synthetic enzymes with novel catalytic properties. Here enzymes featuring a synthetic asymmetric mono-cyanide cofactor have been prepared using two different hydrogenase scaffolds. Their structure and reactivity was in...

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Bibliographic Details
Published in:Chemical science (Cambridge) 2022-09, Vol.13 (37), p.1158-1164
Main Authors: Lorenzi, Marco, Gellett, Joe, Zamader, Afridi, Senger, Moritz, Duan, Zehui, Rodríguez-Maciá, Patricia, Berggren, Gustav
Format: Article
Language:English
Subjects:
Catalysis
Chemical Sciences
Chemistry
Coordination chemistry
Enzymes
Hydrogenase
or physical chemistry
Theoretical and
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Summary:Artificial maturation of hydrogenases provides a path towards generating new semi-synthetic enzymes with novel catalytic properties. Here enzymes featuring a synthetic asymmetric mono-cyanide cofactor have been prepared using two different hydrogenase scaffolds. Their structure and reactivity was investigated in order to elucidate the design rationale behind the native di-cyanide cofactor, and by extension the second coordination sphere of the active-site pocket. Surprisingly, the choice of host enzyme was found to have a dramatic impact on reactivity. Moreover, the study shows that synthetic manipulations of the active-site can significantly increase inhibitor tolerance, as compared to native [FeFe] hydrogenase, while retaining the enzyme's native capacity for reversible catalysis. Cyanide to carbonyl exchange in semi-synthetic [FeFe] hydrogenases: exploring the role of the strong field ligands of the active site and their interaction with the protein matrix via spectroscopy and electrochemistry.
ISSN:2041-6520
2041-6539
2041-6539
DOI:10.1039/d2sc02271k