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Photosynthesis Research

, Volume 98, Issue 1–3, pp 677–685 | Cite as

Artificial photoactive proteins

Review

Abstract

Solar power is the most abundant source of renewable energy. In this respect, the goal of making photoactive proteins is to utilize this energy to generate an electron flow. Photosystems have provided the blueprint for making such systems, since they are capable of converting the energy of light into an electron flow using a series of redox cofactors. Protein tunes the redox potential of the cofactors and arranges them such that their distance and orientation are optimal for the creation of a stable charge separation. The aim of this review is to present an overview of the literature with regard to some elegant functional structures that protein designers have created by introducing cofactors and photoactivity into synthetic proteins.

Keywords

Protein design Photosystem Cofactor binding Chlorophyll Electron transfer Reaction center 

Abbreviations

BChl

Bacteriochlorophyll

Ce6

Chlorin e6

Chl

Chlorophyll

cyt

Cytochrome

ET

Electron transfer

Fe–S

Iron–sulfur cluster

LH

Light-harvesting complex

P

Primary electron donor

Pheo

Pheophytin

PSI

Photosystem I

PSII

Photosystem II

OG

n-Octyl β-d-glycopyranoside

RC

Reaction centre

WSCP

Water-soluble Chl binding proteins

Notes

Acknowledgments

This work was supported in part by Nova Southeastern University Faculty Research and Development Grant.

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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  1. 1.Division of Math, Science, and Technology, Farquhar College of Arts & ScienceNova Southeastern UniversityFort LauderdaleUSA

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