Electronic states of the O2-tolerant [NiFe] hydrogenase proximal cluster
| Autor: | Juan-Carlos Fontecilla-Camps, Patricia Amara, Jean-Marie Mouesca |
|---|---|
| Přispěvatelé: | Magnetic Resonance (RM ), Modélisation et Exploration des Matériaux (MEM), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Hydrogenase
010402 general chemistry 01 natural sciences 03 medical and health sciences Mössbauer spectroscopy Cluster (physics) Symmetry breaking Spin (physics) Hyperfine structure ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences MESH: Iron Multidisciplinary [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Chemistry Quadrupole splitting 0104 chemical sciences MESH: Sulfur Crystallography MESH: Bacteria MESH: Spectroscopy Mossbauer MESH: Hydrogenase MESH: Electron Spin Resonance Spectroscopy Density functional theory Atomic physics MESH: Models Molecular |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (28), pp.E2538-E2538. ⟨10.1073/pnas.1302304110⟩ Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (28), pp.E2538-E2538. ⟨10.1073/pnas.1302304110⟩ |
| ISSN: | 0027-8424 1091-6490 |
| DOI: | 10.1073/pnas.1302304110⟩ |
| Popis: | Recently, Pandelia et al. (1) used density functional theory (DFT) calculations to interpret their Mossbauer experiments on the superoxidized state of the O2-tolerant hydrogenase [4Fe3S] proximal cluster. Experimentally (table 2 in ref. 1), the subspectrum (S) exhibits the largest quadrupole splitting (ΔEQ = 2.45 mm/s) and a positive hyperfine value A , indicating that the corresponding iron ion belongs to the minority spin sites (i.e., the projection coefficient K of its local spin onto the cluster spin is negative). Among the possible DFT broken symmetry (BS) states Oxn\_ij computed to identify this (S) signal [ij: mixed-valence pair; n = 1: nearby protonated glutamate, n = 2: deprotonated Glu], the authors have retained Ox2\_14 and Ox2_24, as we did previously [BS13 and BS34, respectively (2), considering local iron spin alignments only]. Note that changing Fe1→1, Fe2→4 (unique … [↵][1]1To whom correspondence may be addressed. E-mail: jean-marie.mouesca{at}cea.fr or juan.fontecilla{at}ibs.fr. [1]: #xref-corresp-1-1 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|