- Abstract:
-
The redox properties of the blue copper protein amicyanin have been studied with slow and fast scan protein-film cyclic voltammetry. At slow scan rates, which reveal the thermodynamics of the redox reactions, the reduction potential of amicyanin depends on pH in a sigmoidal manner, and the data can be analysed in terms of electron transfer being coupled to a single protonatable group with pKa(red)=6.3 and pKa(ox) < or = 3.2 at 22 degrees C. Voltammetry at higher scan rates reveals the kine...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1007/s007750100269
-
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- Journal:
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
- Volume:
- 7
- Issue:
- 1-2
- Pages:
- 94-100
- Publication date:
- 2002-01-05
- DOI:
- EISSN:
-
1432-1327
- ISSN:
-
0949-8257
- URN:
-
uuid:f572bdfe-2a2c-43a0-a4b8-482e093180bc
- Source identifiers:
-
38134
- Local pid:
- pubs:38134
- Copyright date:
- 2002
Journal article
The pH-dependent redox inactivation of amicyanin from Paracoccus versutus as studied by rapid protein-film voltammetry.
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