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The electrically wired molybdenum domain of human sulfite oxidase is bioelectrocatalytically active

 
: Spricigo, R.; Leimkühler, S.; Gorton, L.; Scheller, F.W.; Wollenberger, U.

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European journal of inorganic chemistry (2015), Nr.21, S.3526-3531
ISSN: 1434-1948
ISSN: 1099-0682
Englisch
Zeitschriftenaufsatz
Fraunhofer IZI ()

Abstract
We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N′-methyl-2,2′-biimidazole)3]2+/3+ complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25 % of the signal of the wired full molybdoheme enzyme hSO, in which the heme b5 is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices.

: http://publica.fraunhofer.de/dokumente/N-352502.html