ArticleThe Journal of biological chemistry2012
Biochemical analysis of the interactions between the proteins involved in the [FeFe]-hydrogenase maturation process.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Role of ammonia-lyases in the synthesis of the dithiomethylamine ligand during [FeFe]-hydrogenase maturation.The Journal of biological chemistry · 2024Article
- Proposed Mechanism for the Biosynthesis of the [FeFe] Hydrogenase H-Cluster: Central Roles for the Radical SAM Enzymes HydG and HydE.ACS bio & med chem Au · 2022Review
- HydG, the "dangler" iron, and catalytic production of free CO and CNDalton transactions (Cambridge, England : 2003) · 2021Article
- Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.Chemical science · 2020Review
- The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.The Journal of biological chemistry · 2020Article
- H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Overview of the Maturation Machinery of the H-Cluster of [FeFe]-Hydrogenases with a Focus on HydF.International journal of molecular sciences · 2018Review
- Structural and functional characterization of the hydrogenase-maturation HydF protein.Nature chemical biology · 2017Article
- Article
- Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch.Scientific reports · 2017Article
- A Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF.Biochemistry · 2016Article
- Cysteine as a ligand platform in the biosynthesis of the FeFe hydrogenase H cluster.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- EPR Spectroscopic Studies of [FeFe]-Hydrogenase Maturation.Catalysis letters · 2015Article
- [FeFe]-hydrogenase maturation: insights into the role HydE plays in dithiomethylamine biosynthesis.Biochemistry · 2015Article
- Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.The Journal of biological chemistry · 2015Review
- H-cluster assembly during maturation of the [FeFe]-hydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Radical S-adenosylmethionine enzymes.Chemical reviews · 2014Review
- Identification of global ferredoxin interaction networks in Chlamydomonas reinhardtii.The Journal of biological chemistry · 2013Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
[FeFe]-hydrogenases are iron-sulfur proteins characterized by a complex active site, the H-cluster, whose assembly requires three conserved maturases. HydE and HydG are radical S-adenosylmethionine enzymes that chemically modify a H-cluster precursor on HydF, a GTPase with a dual role of scaffold on which this precursor is synthesized, and carrier to transfer it to the hydrogenase. Coordinate structural and functional relationships between HydF and the two other maturases are crucial for the H-cluster assembly. However, to date only qualitative analysis of this protein network have been provided. In this work we showed that the interactions of HydE and HydG with HydF are distinct events, likely occurring in a precise functional order driven by different kinetic properties, independently of the HydF GTPase activity, which is instead involved in the dissociation of the maturases from the scaffold. We also found that HydF is able to interact with the hydrogenase only when co-expressed with the two other maturases, indicating that under these conditions it harbors per se all the structural elements needed to transfer the H-cluster precursor, thus completing the maturation process. These results open new working perspectives aimed at improving the knowledge of how these complex metalloenzymes are biosynthesized.
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