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CO and CN- syntheses by [FeFe]-hydrogenase maturase HydG are catalytically differentiated events.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Pagnier, Adrien Martin, Lydie Zeppieri, Laura Nicolet, Yvain Fontecilla-Camps, Juan C. |
| Copyright Year | 2016 |
| Abstract | The synthesis and assembly of the active site [FeFe] unit of [FeFe]-hydrogenases require at least three maturases. The radical S-adenosyl-l-methionine HydG, the best characterized of these proteins, is responsible for the synthesis of the hydrogenase CO and CN(-) ligands from tyrosine-derived dehydroglycine (DHG). We speculated that CN(-) and the CO precursor (-):CO2H may be generated through an elimination reaction. We tested this hypothesis with both wild type and HydG variants defective in second iron-sulfur cluster coordination by measuring the in vitro production of CO, CN(-), and (-):CO2H-derived formate. We indeed observed formate production under these conditions. We conclude that HydG is a multifunctional enzyme that produces DHG, CN(-), and CO at three well-differentiated catalytic sites. We also speculate that homocysteine, cysteine, or a related ligand could be involved in Fe(CO)x(CN)y transfer to the HydF carrier/scaffold. |
| File Format | PDF HTM / HTML |
| DOI | 10.1073/pnas.1515842113 |
| PubMed reference number | 26699472 |
| Journal | Medline |
| Volume Number | 113 |
| Issue Number | 1 |
| Alternate Webpage(s) | http://www.pnas.org/content/113/1/104.full.pdf |
| Alternate Webpage(s) | https://doi.org/10.1073/pnas.1515842113 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
