Issue 39, 2017

Copper induced spin state change of heme–Aβ associated with Alzheimer's disease

Abstract

Heme binds Aβ to give a mixture of a mono-histidine bound high spin peroxidase type active site and a bis-histidine bound low spin cytochrome b type active site present in an equilibrium at physiological pH. Of these, the high spin mono-histidine bound complexes produce significant amounts of partially reduced oxygen species (PROS), catalyze the degradation of neurotransmitters and oxidize cytochrome c, with potentially detrimental effects. The presence of excess Aβ could lower these effects by creating a low spin bis-histidine cytochrome b type active site which exerts less oxidative stress by producing a much smaller amount of PROS. The presence of Cu(II) reverses this effect and can convert the benign low spin heme–Aβ complex to the detrimental high spin form, even in the presence of excess Aβ. Data suggest that the histidine needed to form the bis-histidine site in the low spin heme–Aβ complex is likely to be involved in the high affinity Cu binding site in the heme–Cu–Aβ complex.

Graphical abstract: Copper induced spin state change of heme–Aβ associated with Alzheimer's disease

Supplementary files

Article information

Article type
Communication
Submitted
10 май 2017
Accepted
19 июн 2017
First published
22 июн 2017

Dalton Trans., 2017,46, 13171-13175

Copper induced spin state change of heme–Aβ associated with Alzheimer's disease

S. Mukherjee, C. Ghosh, M. Seal and S. G. Dey, Dalton Trans., 2017, 46, 13171 DOI: 10.1039/C7DT01700F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements