ArticleThe Journal of biological chemistry2012
A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase.
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 30 papers.
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30 citing papers in PubMed, 60 citations in OpenAlex.
- Development of a Universal Platform for the Heterologous Expression of Bidirectional [Ni-Fe]-Hydrogenases inACS synthetic biology · 2025Article
- Biosynthesis and assembly of hydrogenase [NiFe]-cofactor: recent advances and perspectives.Metallomics : integrated biometal science · 2025Review
- Co-expression of auxiliary genes enhances the activity of a heterologous OBiotechnology for biofuels and bioproducts · 2025Article
- ATP-Triggered Fe(CN)Journal of the American Chemical Society · 2024Article
- The energy metabolism ofApplied and environmental microbiology · 2024Article
- Evidence the Isc iron-sulfur cluster biogenesis machinery is the source of iron for [NiFe]-cofactor biosynthesis in Escherichia coli.Scientific reports · 2024Article
- Stepwise assembly of the active site of [NiFe]-hydrogenase.Nature chemical biology · 2023Article
- A redox-active HybG-HypD scaffold complex is required for optimal ATPase activity during [NiFe]-hydrogenase maturation in Escherichia coli.FEBS open bio · 2023Article
- Genome-Scale Mining of Acetogens of the GenusMicrobiology spectrum · 2022Article
- High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase FromFrontiers in microbiology · 2022Article
- Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)Scientific reports · 2021Article
- Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.The Biochemical journal · 2021Article
- Bioassembly of complex iron-sulfur enzymes: hydrogenases and nitrogenases.Nature reviews. Chemistry · 2020Article
- A membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturation.MicrobiologyOpen · 2020Article
- The large subunit of the regulatory [NiFe]-hydrogenase fromChemical science · 2020Article
- The iron-sulfur-containing HypC-HypD scaffold complex of the [NiFe]-hydrogenase maturation machinery is an ATPase.FEBS open bio · 2019Article
- Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy.Chemical science · 2019Article
- Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.Communications biology · 2019Article
- CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogen-cycling [NiFe] hydrogenases harbor a dinuclear catalytic center composed of nickel and iron ions, which are coordinated by four cysteine residues. Three unusual diatomic ligands in the form of two cyanides (CN(-)) and one carbon monoxide (CO) are bound to the iron and apparently account for the complexity of the cofactor assembly process, which involves the function of at least six auxiliary proteins, designated HypA, -B, -C, -D, -E, and -F. It has been demonstrated previously that the HypC, -D, -E, and -F proteins participate in cyanide synthesis and transfer. Here, we show by infrared spectroscopic analysis that the purified HypCD complexes from Ralstonia eutropha and Escherichia coli carry in addition to both cyanides the CO ligand. We present experimental evidence that in vivo the attachment of the CN(-) ligands is a prerequisite for subsequent CO binding. With the aid of genetic engineering and subsequent mutant analysis, the functional role of conserved cysteine residues in HypD from R. eutropha was investigated. Our results demonstrate that the HypCD complex serves as a scaffold for the assembly of the Fe(CN)(2)(CO) entity of [NiFe] hydrogenase.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.