Browse by author
Lookup NU author(s): Dr David Hunter, Dr Katsuko Sato, Emeritus Professor William McFarlane, Professor Christopher Dennison
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
In general, inter-protein electron transfer proceeds via the formation of transient complexes. The initial stage of the interaction between plastocyanin (PCu) and cytochrome f (cyt f) from plants is mediated by complementary electrostatics. Given the diffuse nature of its acidic patch, parsley PCu is an atypical example of a plant PCu. The interaction of this PCu with turnip cyt f was investigated by stopped-flow kinetics, NMR spectroscopy and protein-docking simulations. We show that, despite the altered acidic patch, parsley PCu is as efficient as spinach PCu in accepting electrons from cyt f, over the physiological range of ionic strength. At high ionic strength, the rate constant for the reaction of cyt f with parsley PCu is twice that of the spinach protein. This difference in reactivity is attributed to variations in the hydrophobic patch of parsley PCu. The results of NMR studies and protein-docking simulations indicate that parsley PCu and its spinach analogue adopt different orientations in their complexes with cyt f.
Author(s): Crowley PB, Hunter DM, Sato K, McFarlane W, Dennison C
Publication type: Article
Publication status: Published
Journal: Biochemical Journal
Year: 2004
Volume: 378
Issue: 1
Pages: 45-51
ISSN (print): 0264-6021
ISSN (electronic): 1470-8728
Publisher: Portland Press Ltd
URL: http://dx.doi.org/10.1042/BJ20031423
DOI: 10.1042/BJ20031423
PubMed id: 14585099
Altmetrics provided by Altmetric
