caa a22 4500 605507317 CHVBK 20210128100631.0 cr unu---uuuuu 210128e20150401xx s 000 0 eng 10.1007/s00775-015-1241-y doi (NATIONALLICENCE)springer-10.1007/s00775-015-1241-y Interaction of apoNeuroglobin with heme-Aβ complexes relevant to Alzheimer's disease [Elektronische Daten] [Manas Seal, Sheetal Uppal, Suman Kundu, Somdatta Dey] Heme-Aβ complexes are known to produce toxic partially reduced oxygen species (PROS), catalyze oxidation of neurotransmitters and have been associated with Alzheimer's disease (AD). Neuroglobin (Ngb) play a crucial neuroprotective role against oxidative damage, hypoxic injuries, stroke and apoptosis of neuronal cells. In this study, the interaction of heme-Aβ with apoNeuroglobin (apoNgb) has been investigated using a combination of spectroscopic techniques. Absorption and resonance Raman data confirm that apoNgb can uptake heme from heme-Aβ and constitute a six-coordinate low-spin ferric heme-active site identical to that of Ngb. ApoNgb can also uptake heme from reduced heme-Aβ resulting in the formation of ferrous Ngb. The rate of the heme transfer reaction has been found to be of the order of 106M−1s−1. The reaction is faster for oxidized heme-Aβ than the reduced form. The amount of PROS formation by heme-Aβ complexes has been found to diminish drastically after reaction with apoNgb. ApoNgb can also sequester ligand-bound heme from heme-Aβ, e.g., the CO-bound heme from heme-Aβ-CO complex resulting in the formation of Ngb-CO complex. Additionally, ApoNgb can sequester heme from self-assembled monolayer (SAM) of surface-bound heme-Aβ formed over Au surface. This heme sequestration by apoNgb from heme-Aβ not only diminishes heme-induced toxicity but more significantly it produces Ngb which has well-documented neuroprotective role and can thereby potentially reduce risks associated with AD. Graphical Abstract: SBIC, 2015 Heme-Aβ nationallicence ApoNeuroglobin nationallicence Neuroglobin nationallicence Alzheimer's disease nationallicence PROS nationallicence Seal Manas Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, Jadavpur, 700032, Kolkata, India aut Uppal Sheetal Department of Biochemistry, University of Delhi South Campus, 110021, New Delhi, India aut Kundu Suman Department of Biochemistry, University of Delhi South Campus, 110021, New Delhi, India aut Dey Somdatta Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, Jadavpur, 700032, Kolkata, India aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/3(2015-04-01), 563-574 0949-8257 20:3<563 2015 20 775 https://doi.org/10.1007/s00775-015-1241-y text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-015-1241-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Seal Manas Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, Jadavpur, 700032, Kolkata, India aut NATIONALLICENCE 700 1- Uppal Sheetal Department of Biochemistry, University of Delhi South Campus, 110021, New Delhi, India aut NATIONALLICENCE 700 1- Kundu Suman Department of Biochemistry, University of Delhi South Campus, 110021, New Delhi, India aut NATIONALLICENCE 700 1- Dey Somdatta Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, Jadavpur, 700032, Kolkata, India aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/3(2015-04-01), 563-574 0949-8257 20:3<563 2015 20 775