Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 43, Issue 3, Pages 295-299Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2008.07.003
Keywords
cytochrome c; neuroglobin; molecular docking; surface plasmon resonance; NMR spectroscopy
Funding
- Auckland Medical Research Foundation
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It has recently been proposed that the role of neuroglobin in the protection of neurons from ischaemia induced cell death requires the formation of a transient complex with cytochrome c. No such complex has yet been isolated. Here, we present the results of soft docking calculations, which indicate one major binding site for cytochrome c to neuroglobin. The results yield a plausible structure for the most likely complex structure in which the hemes of each protein are in close contact. NMR analysis identifies the formation of a weak complex in which the heme group of cytochrome c is involved. surface plasmon resonance studies provide a value of 45 mu M for the equilibrium constant for cytochrome c binding to neuroglobin, which increases significantly as the ionic strength of the solution increases. The temperature dependence of the binding constant indicates that the complex formation is associated with a small unfavourable enthalpy change (1.9 kcal mol(-1)) and a moderately large, favourable entropy change (14.8 cal mol(-1) deg(-1)). The sensitivity of the binding constant to the presence of salt suggests that the complex formation involves electrostatic interactions. (C) 2008 Elsevier B.V. All rights reserved.
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