[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Ramasarma, T. and Vaigundan, D. (2019) Connecting CuA with metal centers of heme a, heme a, CuB and Zn by pathways with hydrogen bond as the bridging element in cytochrome c oxidase. Biochemical and Biophysical Research Communications, 510 (2). pp. 261-265. ISSN 0006-291X

[img] Text
BBRC 510 p261.pdf
Restricted to Repository staff only

Download (1749Kb) | Request a copy

Abstract

Pathways formed of delocalized π-electron systems and polar groups of polypeptide chains bridged by hydrogen bonds are referred as π-H pathways. Suitable for electron transfer, these pathways in cytochrome c oxidase connect CuA, the source of electrons distributed in cytochrome c oxidase, with the metal centers, heme a, heme a3, CuB, the constituents of the catalytic binuclear center. The unusually rapid electron transfer between heme a and heme a3 would have been facilitated by the link pathway of a long sequence of alternate peptide unit and hydrogen bond spanning Pro336-Val374, referred as suprahelix, between these hemes. Two pathways between CuA center and zinc center, share some portions with purported proton-translocating channels, designated "K" and "D".

Item Type: Article
Depositing User: Users 2 not found.
Date Deposited: 04 Feb 2019 18:53
Last Modified: 15 Feb 2019 06:13
URI: http://cdfd.sciencecentral.in/id/eprint/883

Actions (login required)

View Item View Item