Flavoproteins are redox proteins, some times photo active that catalyze a wide range of biological reactions in which they can accept or donate one or two electrons.  These functions include O2 activation, dehydrogenation, aromatic hydroxylation and various photo-biological processes such as DNA repair and blue light sensing proteins. This diversity is due to the selection in nature of the redox properties (varying over ~500 mV) of the flavin by specific interactions with the protein moiety.  We aim to understand the basis of this control by design of a single chain tetra-helical protein maquettes in which various synthetic flavins are covalently coupled via cysteine at selected positions.  We present the successful demonstration of light-activated electron transfer to a bis-his ligated heme bound with in the maquette upon light excitation and oxidation of nicotinamide analogues by these different flavomaquettes. These are important steps towards the design of novel photo catalysts and oxidoreductases.

Design and engineering of artificial flavoproteins

244th National Meeting (2012)

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