Ramasarma, T. and Vaigundan, D. (2018) Alternative pathway linked by hydrogen bonds connects heme-Fe of cytochrome c with subunit II-CuA of cytochrome a. Biochemical and Biophysical Research Communications, 505 (2). pp. 445-447. ISSN 0006-291X

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Abstract

The bridging element for electron transfer in proteins is the hydrogen bond according to the new experimental perspective in preference to carbon-carbon σ-bond presently used. The purpose of this study is to identify an alternative pathway linked by hydrogen bonds suitable for electron transfer from heme-Fe of cytochrome c to subunit II-CuA of cytochrome a. A pathway consisting of 15 delocalized electron systems including peptide bonds, 5 polar groups of side chains of amino acid residues and 8 water molecules, linked by 27 hydrogen bonds, exists between the two metal electron centers of heme-Fe of cytochrome c, cytochrome c and of subunit II-CuA of cytochrome a. Pathways built of delocalized π-electron systems, polar groups and water molecules linked by hydrogen bonds may be considered for intramolecular and intermolecular electron transfer in proteins.

Item Type:	Article
Uncontrolled Keywords:	Electron transfer; Carbon-carbon σ-bonds
Depositing User:	Users 2 not found.
Date Deposited:	08 Oct 2018 18:17
Last Modified:	18 Oct 2018 09:35
URI:	http://cdfd.sciencecentral.in/id/eprint/865

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