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The pH-dependent redox inactivation of amicyanin from Paracoccus versutus as studied by rapid protein-film voltammetry.

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...

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Publication status:
Published

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Publisher copy:
10.1007/s007750100269

Authors


Jeuken, LC More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Canters, GW More by this author
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

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