Designing photosystem II: Molecular engineering of photo-catalytic proteins

Brendon Conlan*

*Corresponding author for this work

    Research output: Contribution to journalReview articlepeer-review

    17 Citations (Scopus)

    Abstract

    Biological photosynthesis utilizes membrane-bound pigment/protein complexes to convert light into chemical energy through a series of electron-transfer events. In the unique photosystem II (PSII) complex these electron-transfer events result in the oxidation of water to molecular oxygen. PSII is an extremely complex enzyme and in order to exploit its unique ability to convert sunlight into chemical energy it will be necessary to make a minimal model. Here we will briefly describe how PSII functions and identify those aspects that are essential in order to catalyze the oxidation of water into O2, and review previous attempts to design simple photo-catalytic proteins and summarize our current research exploiting the E. coli bacterioferritin protein as a scaffold into which multiple cofactors can be bound, to oxidize a manganese metal center upon illumination. Through the reverse engineering of PSII and light driven water splitting reactions it may be possible to provide a blueprint for catalysts that can produce clean green fuel for human energy needs.

    Original languageEnglish
    Pages (from-to)687-700
    Number of pages14
    JournalPhotosynthesis Research
    Volume98
    Issue number1-3
    DOIs
    Publication statusPublished - Oct 2008

    Fingerprint

    Dive into the research topics of 'Designing photosystem II: Molecular engineering of photo-catalytic proteins'. Together they form a unique fingerprint.

    Cite this