Alternative pathway linked by hydrogen bonds connects heme-Fe of cytochrome c with subunit II-CuA of cytochrome a

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. In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 505 (2). pp. 445-447.

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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 sigma-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 pi-electron systems, polar groups and water molecules linked by hydrogen bonds may be considered for intramolecular and intermolecular electron transfer in proteins. (C) 2018 Elsevier Inc. All rights reserved.

Item Type:	Journal Article
Publication:	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Publisher:	ACADEMIC PRESS INC ELSEVIER SCIENCE
Additional Information:	Copy right for this article belong to ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords:	Cytochrome c; Heme-Fe; Subunit II-CuA; Electron transfer; Hydrogen bonds; Carban-carbon sigma-bonds
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	22 Nov 2018 15:04
Last Modified:	22 Nov 2018 15:04
URI:	http://eprints.iisc.ac.in/id/eprint/61115

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