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  How the dynamics of the metal-binding loop region controls the acid transition in cupredoxins.

Paltrinieri, L., Borsari, M., Battistuzzi, G., Sola, M., Dennison, C., de Groot, B. L., et al. (2013). How the dynamics of the metal-binding loop region controls the acid transition in cupredoxins. Biochemistry, 52(42), 7397-7404. doi:10.1021/bi400860n.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-B41E-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CB8F-0
Genre: Journal Article

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http://pubs.acs.org/doi/pdf/10.1021/bi400860n (Publisher version)
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Paltrinieri, L., Author
Borsari, M., Author
Battistuzzi, G., Author
Sola, M., Author
Dennison, C., Author
de Groot, B. L.1, Author              
Corni, S., Author
Bortolotti, C. A., Author
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1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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 Abstract: Many reduced cupredoxins undergo a pH-dependent structural rearrangement, triggered by protonation of the His ligand belonging to the C-terminal hydrophobic loop, usually termed the acid transition. At variance with several members of the cupredoxin family, the acid transition is not observed for azurin (AZ). We have addressed this issue by performing molecular dynamics simulations of AZ and four mutants, in which the C-terminal loop has been replaced with those of other cupredoxins or with polyalanine loops. All of the loop mutants undergo the acid transition in the pH range of 4.4-5.5. The main differences between AZ and its loop mutants are the average value of the active site solvent accessible surface area and the extent of its fluctuations with time, together with an altered structure of the water layer around the copper center. Using functional mode analysis, we found that these variations arise from changes in nonbonding interactions in the second coordination sphere of the copper center, resulting from the loop mutation. Our results strengthen the view that the dynamics at the site relevant for function and its surroundings are crucial for protein activity and for metal-containing electron transferases.

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Language(s): eng - English
 Dates: 2013-09-242013-10-22
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/bi400860n
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Title: Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 52 (42) Sequence Number: - Start / End Page: 7397 - 7404 Identifier: -