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Hemin, copper and amyloid-β: A medley involved in Alzheimer's disease. An interaction that fine regulates the reactivity.
J Inorg Biochem
February 2025
Dipartimento di Chimica, Università di Pavia, Via Taramelli 12, 27100 Pavia, Italy. Electronic address:
Metal ions have been shown to play a critical role in amyloid-β (Aβ) neurotoxicity and plaque formation which are key hallmarks of Alzheimer's disease. Amyloid-β peptides can bind both copper and hemin and this interaction modulates the redox chemistry of these metals. The characterization of the binding of hemin through UV-Vis spectroscopic titration with Aβ(4-16) shows a significantly higher affinity than that with Aβ(1-16).
View Article and Find Full Text PDFBridge vs Terminal Cyano-coordination in Binuclear Cobalt Porphyrin Dimers: Interplay of Electrons between Metal and Ligand and Spin-Coupling via Bridge.
Inorg Chem
August 2024
Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Three cyano-coordinated cobalt porphyrin dimers were synthesized and thoroughly characterized. The X-ray structure of the complexes reveals that cyanide binds in a terminal fashion in both the and isomers of ethane- and ethylene-bridged cobalt porphyrin dimers, while in the ethylene-bridged dimer, cyanides bind in both terminal and bridging modes. The nonconjugated ethane-bridged complex stabilizes exclusively a diamagnetic metal-centered oxidation of type Co(por)(CN) both in the solid and in solution.
View Article and Find Full Text PDFProton transfer in cytochrome bd-I from E. coli involves Asp-105 in CydB.
Biochim Biophys Acta Bioenerg
November 2024
Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. Electronic address:
Cytochrome bds are bacterial terminal oxidases expressed under low oxygen conditions, and they are important for the survival of many pathogens and hence potential drug targets. The largest subunit CydA contains the three redox-active cofactors heme b, heme b and the active site heme d. One suggested proton transfer pathway is found at the interface between the CydA and the other major subunit CydB.
View Article and Find Full Text PDFTerminal Hydride Complex of High-Spin Mn.
J Am Chem Soc
July 2024
Department of Chemistry, Tulane University, New Orleans, Louisiana 70118, United States.
The iron-molybdenum cofactor of nitrogenase (FeMoco) catalyzes fixation of N via Fe hydride intermediates. Our understanding of these species has relied heavily on the characterization of well-defined 3d metal hydride complexes, which serve as putative spectroscopic models. Although the Fe ions in FeMoco, a weak-field cluster, are expected to adopt locally high-spin Fe configurations, synthetically accessible hydride complexes featuring d or d electron counts are almost exclusively low-spin.
View Article and Find Full Text PDFMolybdenum(VI) Nitrido Complexes with Tripodal Silanolate Ligands. Structure and Electronic Character of an Unsymmetrical Dimolybdenum μ-Nitrido Complex Formed by Incomplete Nitrogen Atom Transfer.
Inorg Chem
May 2024
Max-Planck-Institut für Kohlenforschung, 45470 Mülheim/Ruhr, Germany.
In contrast to a tungsten nitrido complex endowed with a tripodal silanolate ligand framework, which was reported in the literature to be a dimeric species with a metallacyclic core, the corresponding molybdenum nitrides are monomeric entities comprising a regular terminal nitride unit, as proven by single-crystal X-ray diffraction (SC-XRD). Their electronic character is largely determined by the constraints imposed on the metal center by the podand ligand architecture. Mo nuclear magnetic resonance (NMR) and, to a lesser extent, N NMR spectroscopy allow these effects to be studied, which become particularly apparent upon comparison with the spectral data of related molybdenum nitrides comprising unrestrained silanolate, alkoxide, or amide ligands.
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