Intermolecular Interactions and Intramolecular Couplings of Binuclear Porphyrin Models for Cytochrome c Oxidase.
Zhen YaoCharles E SchulzJiahui YangXiangjun LiJianfeng LiPublished in: Inorganic chemistry (2020)
Cytochrome c oxidase (CcO) has a binuclear active site composed of a high-spin heme group and a tris-histidine-ligated copper ion (CuB). By using two different porphyrin models derived by Gunter (H2TPyPP) and us (H2TImPP), we have isolated several mono- and binuclear complexes including one carbonyl and three chloride derivatives which are determined by 100 K single-crystal X-ray. Low-temperature (4 K) EPR and multitemperature (295-25 K) Mössbauer investigations on the products not only confirmed the spin states of the two metal ions (S = 5/2 Fe3+ and S = 1/2 Cu2+) but also revealed the intermolecular interactions and intramolecular couplings which are in accordance with the crystal structural features.
Keyphrases
- energy transfer
- quantum dots
- metal organic framework
- aqueous solution
- room temperature
- density functional theory
- single molecule
- photodynamic therapy
- high resolution
- single cell
- transition metal
- solid state
- mass spectrometry
- computed tomography
- magnetic resonance imaging
- ionic liquid
- oxide nanoparticles
- water soluble
- electron transfer