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Fully Refined Semisynthesis of the [FeFe] Hydrogenase H-Cluster
- Source :
- Biochemistry; October 2023, Vol. 62 Issue: 19 p2868-2877, 10p
- Publication Year :
- 2023
-
Abstract
- [FeFe] hydrogenases contain a 6-Fe cofactor that serves as the active site for efficient redox interconversion between H2and protons. The biosynthesis of the so-called H-cluster involves unusual enzymatic reactions that synthesize organometallic Fe complexes containing azadithiolate, CO, and CN–ligands. We have previously demonstrated that specific synthetic [Fe(CO)x(CN)y] complexes can be used to functionally replace proposed Fe intermediates in the maturation reaction. Here, we report the results from performing such cluster semisynthesis in the context of a recent fully defined cluster maturation procedure, which eliminates unknown components previously employed from Escherichia colicell lysate and demonstrate this provides a concise route to H-cluster synthesis. We show that formaldehyde can be used as a simple reagent as the carbon source of the bridging adt ligand of H-cluster in lieu of serine/serine hydroxymethyltransferase. In addition to the actual H-cluster, we observe the formation of several H-cluster-like species, the identities of which are probed by cryogenic photolysis combined with EPR/ENDOR spectroscopy.
Details
- Language :
- English
- ISSN :
- 00062960 and 15204995
- Volume :
- 62
- Issue :
- 19
- Database :
- Supplemental Index
- Journal :
- Biochemistry
- Publication Type :
- Periodical
- Accession number :
- ejs63871429
- Full Text :
- https://doi.org/10.1021/acs.biochem.3c00393