Ramasarma, T and Vaigundan, D (2019) Connecting CuA with metal centers of heme a, heme a(3), CuB and Zn by pathways with hydrogen bond as the bridging element in cytochrome c oxidase. In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 510 (2). pp. 261-265.
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Abstract
Pathways formed of delocalized pi-electron systems and polar groups of polypeptide chains bridged by hydrogen bonds are referred as pi-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 a(3), CuB, the constituents of the catalytic binuclear center. The unusually rapid electron transfer between heme a and heme a(3) 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''. (C) 2019 Elsevier Inc. All rights reserved.
Item Type: | Journal Article |
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Publication: | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
Publisher: | ACADEMIC PRESS INC ELSEVIER SCIENCE |
Additional Information: | Copyright of this article belongs to ACADEMIC PRESS INC ELSEVIER SCIENCE |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 26 Mar 2019 06:41 |
Last Modified: | 26 Mar 2019 06:41 |
URI: | http://eprints.iisc.ac.in/id/eprint/61922 |
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