ArticleThe Journal of biological chemistry2011
Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 36 citations in OpenAlex.
- 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
- High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase FromFrontiers in microbiology · 2022Article
- A membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturation.MicrobiologyOpen · 2020Article
- 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
- Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structure, function and biosynthesis of O₂-tolerant hydrogenases.Nature reviews. Microbiology · 2013Review
- Comparative genomic analyses of the cyanobacterium, Lyngbya aestuarii BL J, a powerful hydrogen producer.Frontiers in microbiology · 2013Article
- A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase.The Journal of biological chemistry · 2012Article
- Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum.BMC microbiology · 2012Article
- Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases.The Journal of biological chemistry · 2012Article
- Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an OChemical scienceArticle
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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
The O(2)-tolerant [NiFe] hydrogenases of Ralstonia eutropha are capable of H(2) conversion in the presence of ambient O(2). Oxygen represents not only a challenge for catalysis but also for the complex assembling process of the [NiFe] active site. Apart from nickel and iron, the catalytic center contains unusual diatomic ligands, namely two cyanides (CN(-)) and one carbon monoxide (CO), which are coordinated to the iron. One of the open questions of the maturation process concerns the origin and biosynthesis of the CO group. Isotope labeling in combination with infrared spectroscopy revealed that externally supplied gaseous (13)CO serves as precursor of the carbonyl group of the regulatory [NiFe] hydrogenase in R. eutropha. Corresponding (13)CO titration experiments showed that a concentration 130-fold higher than ambient CO (0.1 ppmv) caused a 50% labeling of the carbonyl ligand in the [NiFe] hydrogenase, leading to the conclusion that the carbonyl ligand originates from an intracellular metabolite. A novel setup allowed us to the study effects of CO depletion on maturation in vivo. Upon induction of CO depletion by addition of the CO scavenger PdCl(2), cells cultivated on H(2), CO(2), and O(2) showed severe growth retardation at low cell concentrations, which was on the basis of partially arrested hydrogenase maturation, leading to reduced hydrogenase activity. This suggests gaseous CO as a metabolic precursor under these conditions. The addition of PdCl(2) to cells cultivated heterotrophically on organic substrates had no effect on hydrogenase maturation. These results indicate at least two different pathways for biosynthesis of the CO ligand of [NiFe] hydrogenase.
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