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Photo-catalytic oxidation of a di-nuclear manganese centre in an engineered bacterioferritin 'reaction centre'
Australian National University, Canberra, Australia.
Australian National University, Canberra, Australia.
Max Planck Institute for Bioinorganic Chemistry, Mülheim an der Ruhr, Germany.
Australian National University, Canberra, Australia.
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2009 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, Vol. 1787, no 9, 1112-1121 p.Article in journal (Refereed) Published
Abstract [en]

Photosynthesis involves the conversion of light into chemical energy through a series of electron transfer reactions within membrane-bound pigment/protein complexes. The Photosystem II (PSII) complex in plants, algae and cyanobacteria catalyse the oxidation of water to molecular O(2). The complexity of PSII has thus far limited attempts to chemically replicate its function. Here we introduce a reverse engineering approach to build a simple, light-driven photo-catalyst based on the organization and function of the donor side of the PSII reaction centre. We have used bacterioferritin (BFR) (cytochrome b1) from Escherichia coli as the protein scaffold since it has several, inherently useful design features for engineering light-driven electron transport. Among these are: (i.) a di-iron binding site; (ii.) a potentially redox-active tyrosine residue; and (iii.) the ability to dimerise and form an inter-protein heme binding pocket within electron tunnelling distance of the di-iron binding site. Upon replacing the heme with the photoactive zinc-chlorin e(6) (ZnCe(6)) molecule and the di-iron binding site with two manganese ions, we show that the two Mn ions bind as a weakly coupled di-nuclear Mn(2)(II,II) centre, and that ZnCe(6) binds in stoichiometric amounts of 1:2 with respect to the dimeric form of BFR. Upon illumination the bound ZnCe(6) initiates electron transfer, followed by oxidation of the di-nuclear Mn centre possibly via one of the inherent tyrosine residues in the vicinity of the Mn cluster. The light dependent loss of the Mn(II) EPR signals and the formation of low field parallel mode Mn EPR signals are attributed to the formation of Mn(III) species. The formation of the Mn(III) is concomitant with consumption of oxygen. Our model is the first artificial reaction centre developed for the photo-catalytic oxidation of a di-metal site within a protein matrix which potentially mimics WOC photo-assembly.

Place, publisher, year, edition, pages
Elsevier , 2009. Vol. 1787, no 9, 1112-1121 p.
Keyword [en]
Artificial photosynthesis, EPR, Manganese, Electron transfer, Protein engineering, Bacterioferritin, Zinc chlorin e6
National Category
Chemical Sciences
URN: urn:nbn:se:umu:diva-22629DOI: 10.1016/j.bbabio.2009.04.011PubMedID: 19409368OAI: diva2:217452
Available from: 2009-05-14 Created: 2009-05-14 Last updated: 2012-08-07Bibliographically approved

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Messinger, Johannes
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