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| Content Provider | Springer Nature Link |
|---|---|
| Author | Battistuzzi, Gianantonio Bellei, Marzia Dennison, Christopher Di Rocco, Giulia Sato, Katsuko Sola, Marco Yanagisawa, Sachiko |
| Copyright Year | 2007 |
| Abstract | The thermodynamics of the alkaline transition which influences the spectral and redox properties of the type 1 copper center in phytocyanins has been determined spectroscopically. The proteins investigated include Rhus vernicifera stellacyanin, cucumber basic protein and its Met89Gln variant, and umecyanin, the stellacyanin from horseradish roots, along with its Gln95Met variant. The changes in reaction enthalpy and entropy within the protein series show partial compensatory behavior. Thus, the reaction free energy change (hence the pK a value) is rather variable. This indicates that species-dependent differences in reaction thermodynamics, although containing an important contribution from changes in the hydrogen-bonding network of water molecules in the hydration sphere of the protein (which feature enthalpy–entropy compensation), are to a large extent protein-based. The data for axial ligand variants are consistent with the hypothesis of a copper-binding His as the deprotonating residue responsible for this transition. |
| Starting Page | 895 |
| Ending Page | 900 |
| Page Count | 6 |
| File Format | |
| ISSN | 09498257 |
| Journal | JBIC Journal of Biological Inorganic Chemistry |
| Volume Number | 12 |
| Issue Number | 6 |
| e-ISSN | 14321327 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2007-06-15 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Alkaline transition Thermodynamics Electron transfer Phytocyanins Cupredoxins Microbiology Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
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