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Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima .
- Source :
-
Chemical science [Chem Sci] 2023 Feb 27; Vol. 14 (13), pp. 3682-3692. Date of Electronic Publication: 2023 Feb 27 (Print Publication: 2023). - Publication Year :
- 2023
-
Abstract
- [FeFe] hydrogenases are exceptionally active catalysts for the interconversion of molecular hydrogen with protons and electrons. Their active site, the H-cluster, is composed of a [4Fe-4S] cluster covalently linked to a unique [2Fe] subcluster. These enzymes have been extensively studied to understand how the protein environment tunes the properties of the Fe ions for efficient catalysis. The sensory [FeFe] hydrogenase (HydS) from Thermotoga maritima has low activity and displays a very positive redox potential for the [2Fe] subcluster compared to that of the highly active prototypical enzymes. Using site directed mutagenesis, we investigate how second coordination sphere interactions of the protein environment with the H-cluster in HydS influence the catalytic, spectroscopic and redox properties of the H-cluster. In particular, mutation of the non-conserved serine 267, situated between the [4Fe-4S] and [2Fe] subclusters, to methionine (conserved in prototypical catalytic enzymes) gave a dramatic decrease in activity. Infra-red (IR) spectroelectrochemistry revealed a 50 mV lower redox potential for the [4Fe-4S] subcluster in the S267M variant. We speculate that this serine forms a hydrogen bond to the [4Fe-4S] subcluster, increasing its redox potential. These results demonstrate the importance of the secondary coordination sphere in tuning the catalytic properties of the H-cluster in [FeFe] hydrogenases and reveal a particularly important role for amino acids interacting with the [4Fe-4S] subcluster.<br />Competing Interests: There are no conflicts to declare.<br /> (This journal is © The Royal Society of Chemistry.)
Details
- Language :
- English
- ISSN :
- 2041-6520
- Volume :
- 14
- Issue :
- 13
- Database :
- MEDLINE
- Journal :
- Chemical science
- Publication Type :
- Academic Journal
- Accession number :
- 37006680
- Full Text :
- https://doi.org/10.1039/d2sc06432d