Topic
Cubane
About: Cubane is a research topic. Over the lifetime, 1986 publications have been published within this topic receiving 50308 citations. The topic is also known as: pentacyclo[4.2.0.0(2,5).0(3,8).0(4,7)]octane.
Papers published on a yearly basis
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Papers
TL;DR: A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined, providing insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.
Abstract: A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined to 1.8 angstrom resolution by x-ray crystallography using multiwavelength anomalous dispersion (MAD) phasing. CpI, an enzyme that catalyzes the two-electron reduction of two protons to yield dihydrogen, was found to contain 20 gram atoms of iron per mole of protein, arranged into five distinct [Fe-S] clusters. The probable active-site cluster, previously termed the H-cluster, was found to be an unexpected arrangement of six iron atoms existing as a [4Fe-4S] cubane subcluster covalently bridged by a cysteinate thiol to a [2Fe] subcluster. The iron atoms of the [2Fe] subcluster both exist with an octahedral coordination geometry and are bridged to each other by three non-protein atoms, assigned as two sulfide atoms and one carbonyl or cyanide molecule. This structure provides insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.
1,826 citations
TL;DR: In this article, the interconnections among orbital interactions, electron delocalization and spin coupling in iron-sulfur clusters are reviewed, with special attention to the complex nature of spin and orbital states in 4Fe4S complexes.
722 citations
TL;DR: In this article, the preparation, characterization, and X-ray structure for the single-molecule magnet (PPh4)[Mn12O12(O2CPh)16(H2O)4]·8(CH2Cl2) (2) was reported.
Abstract: The preparation, characterization, and X-ray structure are reported for the single-molecule magnet (PPh4)[Mn12O12(O2CPh)16(H2O)4]·8(CH2Cl2) (2). Complex 2 crystallizes in the triclinic space group P1, which at 213 K has a = 17.2329(2), b = 17.8347(2), c = 26.8052(2) A, α = 90.515(2), β = 94.242(2), γ = 101.437(2)°, and Z = 2. The salt consists of PPh4+ cations and [Mn12O12(O2CPh)16(H2O)4]- anions. The (Mn12O12)15+ core of the anion is formed by an external ring of eight Mn atoms bridged by μ3−O2- ions to an internal tetrahedron of four Mn atoms. Because of disorder in both phenyl rings and solvate molecules, it was difficult to use bond valence sum values to determine definitively the oxidation state of each Mn atom. There is a Mn4O4 cubane unit in the internal part of the molecule and these Mn atoms are all MnIV ions. For the eight “external” Mn atoms the bond valence sum values did not define well their oxidation states. For these eight Mn atoms, it was not possible to determine whether a trapped-valen...
546 citations
TL;DR: A rational synthesis of a [Mn3CaO4]6+ cubane is reported that structurally models the trimanganese-calcium–cubane subsite of the OEC, revealing potential roles of calcium in facilitating high oxidation states at manganese and in the assembly of the biological cluster.
Abstract: Within photosynthetic organisms, the oxygen-evolving complex (OEC) of photosystem II generates dioxygen from water using a catalytic Mn_(4)CaOn cluster (n varies with the mechanism and nature of the intermediate). We report here the rational synthesis of a [Mn_(3)CaO_4]^(6+) cubane that structurally models the trimanganese-calcium–cubane subsite of the OEC. Structural and electrochemical comparison between Mn_(3)CaO_4 and a related Mn_(4)O_4 cubane alongside characterization of an intermediate calcium-manganese multinuclear complex reveals potential roles of calcium in facilitating high oxidation states at manganese and in the assembly of the biological cluster.
537 citations
TL;DR: A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica and suggests a newly discovered role for copper in biology.
Abstract: A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum ). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe 4 S 4 ] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.
531 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 30 |
| 2024 | 37 |
| 2023 | 59 |
| 2022 | 82 |
| 2021 | 68 |
| 2020 | 54 |