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Electrochemical characterisation of Formate dehydrogenase and its catalytic properties
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Orientador(es)
Resumo(s)
In recent years the amount of CO2 release into the planet atmosphere has increase
exponentially due to a global dependency in fossil fuels. This is one of the major contributors to the
climate change that is seen nowadays. On the other hand, due to the CO2 abundance, there has been
an interest in developing methods to harvest and use this CO2 in the production of green energy and
sustainable chemistry.
Formate dehydrogenase (FDH) proteins are a class of metalloenzymes with different subunit
composition containing either molybdenum or tungsten at the active site. FDH catalyses the oxidation
of formate into CO2. Recently it was shown that some of the FDH enzymes have the ability to perform
the reverse reaction that is, these can catalyse the reversible interconversion of CO2 and formate.
However, to date, the electrochemical characterisation of the protein has not yet been attained
using direct, non-mediated methods. In this thesis the isolation of FDH from Desulfovibrio desulfuricans,
its biochemical and non-mediated electrochemical characterisation was attained. The redox features of
the Mo catalytic centre of the enzyme, including thermodynamic and kinetic parameters such as its
formal reduction potential (E0’ = -245 ± 8 mV vs NHE) and heterogeneous electron transfer constant,
were determined, for the first time, using direct electrochemical methods. The catalytic activity towards
the CO2 reduction was also observed, for the first time, by direct electrochemical techniques.
Descrição
Palavras-chave
Formate dehydrogenase Bioelectrochemistry Enzymatic catalysis CO2 Reduction