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Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding

Beckerson, P and Reeder, BJ and Wilson, MT (2015) 'Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding.' FEBS Letters, 589 (4). 507 - 512. ISSN 0014-5793

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Abstract

© 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38-C83) alters the dissociation rate constant of the intrinsic histidine (H81) (∼1000 fold), thus controlling binding of extrinsic ligands. Through time-resolved spectra we have unequivocally assigned CO binding to hexa- and penta-coordinate forms and have made direct measurement of histidine rebinding following photolysis. We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding.

Item Type: Article
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Brandon Reeder
Date Deposited: 23 Mar 2015 13:10
Last Modified: 06 Sep 2019 11:15
URI: http://repository.essex.ac.uk/id/eprint/13374

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