Transient protein interactions: the case of
pseudoazurin and nitrite reductase
Impagliazzo, Antonietta
Citation
Impagliazzo, A. (2005, April 7). Transient protein interactions:
the case of pseudoazurin and nitrite reductase. Retrieved from
https://hdl.handle.net/1887/828
Version: Corrected Publisher’s Version
License:
Licence agreement concerning inclusion of doctoral thesis in the Institutional Repository of the University of Leiden
Downloaded from: https://hdl.handle.net/1887/828
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STELLINGEN Behorende bij het proefschrift:
Transient interactions:
The case of pseudoazurin and nitrite reductase Antonietta Impagliazzo
1. The binding of pseudoazurin to nitrite reductase depends on the oxidation state copper ion in pseudoazurin.
(Chapter 3 of this thesis)
2. Protonation of the surface exposed histidine 6 does not explain the presence of two binding modes between reduced pseudoazurin and nitrite reductase.
(Chapter 4 of this thesis) 3. The oxidation state of the copper ion in pseudoazurin affects the orientation of histidine 81, which influences complex formation with nitrite reductase.
(Chapter 5 of this thesis) 4. Hydrophobic as well as electrostatic interactions are important for
pseudoazurin and nitrite reductase complex formation.
(Kukimoto, Protein Engineering, (1995), 8, 153-158 and Chapter V-VI of this thesis) 5. Surface charge compatibility between proteins does not imply
complex formation.
(Boulanger, Journal of Molecular Biology, (2002),315,1111-1127 and Chapter VII of this thesis) 6. Pseudoazurin conformational change between oxidized and
reduced state and their different binding to nitrite reductase is consistent with a system that needs to have an efficient ET with a high turn-over rate.
7. Azurin and nitrite reductase from Neisseria gonorrhoeae react via a collisional mechanism.
(Chapter VII this thesis) 8. Scientific research is not about seeing what everybody sees but
thinking what nobody has thought yet.
9. God gave us two ears but only one mouth, so that we might listen twice as much as we speak.
