ArticleProceedings of the National Academy of Sciences of the United States of America2013
Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 24 citations in OpenAlex.
- The arginine synthetase pathway is responsible for carbamoyl phosphate synthesis inFrontiers in microbiology · 2026Article
- A conserved aspartate residue in [4Fe-4S]-containing HypD is required for [NiFe]-cofactor biosynthesis and for efficient interaction of the HypCD scaffold complex with HypE.Metallomics : integrated biometal science · 2025Article
- Biosynthesis and assembly of hydrogenase [NiFe]-cofactor: recent advances and perspectives.Metallomics : integrated biometal science · 2025Review
- ATP-Triggered Fe(CN)Journal of the American Chemical Society · 2024Article
- An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.Folia microbiologica · 2020Review
- Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.Communications biology · 2019Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Distribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey.Frontiers in genetics · 2016Article
- Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production.Frontiers in microbiology · 2015Article
- Article
- The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.PloS one · 2014Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Hydrogenase pleiotropically acting protein (Hyp)E plays a role in biosynthesis of the cyano groups for the NiFe(CN)2CO center of [NiFe] hydrogenases by catalyzing the ATP-dependent dehydration of the carbamoylated C-terminal cysteine of HypE to thiocyanate. Although structures of HypE proteins have been determined, until now there has been no structural evidence to explain how HypE dehydrates thiocarboxamide into thiocyanate. Here, we report the crystal structures of the carbamoylated and cyanated forms of HypE from Thermococcus kodakarensis in complex with nucleotides at 1.53- and 1.64-Å resolution, respectively. Carbamoylation of the C-terminal cysteine (Cys338) of HypE by chemical modification is clearly observed in the present structures. In the presence of ATP, the thiocarboxamide of Cys338 is successfully dehydrated into the thiocyanate. In the carbamoylated state, the thiocarboxamide nitrogen atom of Cys338 is close to a conserved glutamate residue (Glu272), but the spatial position of Glu272 is less favorable for proton abstraction. On the other hand, the thiocarboxamide oxygen atom of Cys338 interacts with a conserved lysine residue (Lys134) through a water molecule. The close contact of Lys134 with an arginine residue lowers the pKa of Lys134, suggesting that Lys134 functions as a proton acceptor. These observations suggest that the dehydration of thiocarboxamide into thiocyanate is catalyzed by a two-step deprotonation process, in which Lys134 and Glu272 function as the first and second bases, respectively.
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