ArticleProceedings of the National Academy of Sciences of the United States of America2013
Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mossbauer and EPR spectroscopy.
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 17 papers.
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17 citing papers in PubMed.
- Transition metal ions and neurotransmitters: coordination chemistry and implications for neurodegeneration.RSC chemical biology · 2023Review
- Cluster-selectiveChemical science · 2023Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- The large subunit of the regulatory [NiFe]-hydrogenase fromChemical science · 2020Article
- Mixed valency in ligand-bridged diruthenium frameworks: divergences and perspectives.RSC advances · 2018Review
- Conserved Histidine Adjacent to the Proximal Cluster Tunes the Anaerobic Reductive Activation ofChemElectroChem · 2018Article
- Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.Journal of the American Chemical Society · 2017Article
- The EcoCyc database: reflecting new knowledge about Escherichia coli K-12.Nucleic acids research · 2017Article
- Mechanism of ONature chemistry · 2017Article
- Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.Angewandte Chemie (International ed. in English) · 2016Article
- Unanticipated coordination of tris buffer to the Radical SAM cluster of the RimO methylthiotransferase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Models of the Ni-L and Ni-SIa States of the [NiFe]-Hydrogenase Active Site.Inorganic chemistry · 2016Article
- The Mössbauer Parameters of the Proximal Cluster of Membrane-Bound Hydrogenase Revisited: A Density Functional Theory Study.Journal of chemical theory and computation · 2016Article
- Reversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenase.Nature chemical biology · 2014Article
- Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate: quinone reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Reply to Mouesca et al.: Electronic structure of the proximal [4Fe-3S] cluster of O2-tolerant [NiFe] hydrogenases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Electronic states of the O2-tolerant [NiFe] hydrogenase proximal cluster.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Abstract
Iron-sulfur clusters are ubiquitous electron transfer cofactors in hydrogenases. Their types and redox properties are important for H(2) catalysis, but, recently, their role in a protection mechanism against oxidative inactivation has also been recognized for a [4Fe-3S] cluster in O(2)-tolerant group 1 [NiFe] hydrogenases. This cluster, which is uniquely coordinated by six cysteines, is situated in the proximity of the catalytic [NiFe] site and exhibits unusual redox versatility. The [4Fe-3S] cluster in hydrogenase (Hase) I from Aquifex aeolicus performs two redox transitions within a very small potential range, forming a superoxidized state above +200 mV vs. standard hydrogen electrode (SHE). Crystallographic data has revealed that this state is stabilized by the coordination of one of the iron atoms to a backbone nitrogen. Thus, the proximal [4Fe-3S] cluster undergoes redox-dependent changes to serve multiple purposes beyond classical electron transfer. In this paper, we present field-dependent (57)Fe-Mössbauer and EPR data for Hase I, which, in conjunction with spectroscopically calibrated density functional theory (DFT) calculations, reveal the distribution of Fe valences and spin-coupling schemes for the iron-sulfur clusters. The data demonstrate that the electronic structure of the [4Fe-3S] core in its three oxidation states closely resembles that of corresponding conventional [4Fe-4S] cubanes, albeit with distinct differences for some individual iron sites. The medial and distal iron-sulfur clusters have similar electronic properties as the corresponding cofactors in standard hydrogenases, although their redox potentials are higher.
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