Literature DB >> 18830805

Artificial photoactive proteins.

Reza Razeghifard1.   

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.

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Year:  2008        PMID: 18830805     DOI: 10.1007/s11120-008-9367-1

Source DB:  PubMed          Journal:  Photosynth Res        ISSN: 0166-8595            Impact factor:   3.573


  63 in total

1.  Sliding helix and change of coordination geometry in a model di-MnII protein.

Authors:  William F DeGrado; Luigi Di Costanzo; Silvano Geremia; Angela Lombardi; Vincenzo Pavone; Lucio Randaccio
Journal:  Angew Chem Int Ed Engl       Date:  2003-01-27       Impact factor: 15.336

2.  Artificial diiron proteins: from structure to function.

Authors:  Jennifer R Calhoun; Flavia Nastri; Ornella Maglio; Vincenzo Pavone; Angela Lombardi; William F DeGrado
Journal:  Biopolymers       Date:  2005       Impact factor: 2.505

3.  Initial electron donor and acceptor in isolated Photosystem II reaction centers identified with femtosecond mid-IR spectroscopy.

Authors:  Marie Louise Groot; Natalia P Pawlowicz; Luuk J G W van Wilderen; Jacques Breton; Ivo H M van Stokkum; Rienk van Grondelle
Journal:  Proc Natl Acad Sci U S A       Date:  2005-08-31       Impact factor: 11.205

4.  Introduction of a [4Fe-4S (S-cys)4]+1,+2 iron-sulfur center into a four-alpha helix protein using design parameters from the domain of the Fx cluster in the Photosystem I reaction center.

Authors:  M P Scott; J Biggins
Journal:  Protein Sci       Date:  1997-02       Impact factor: 6.725

5.  Myoglobin with modified tetrapyrrole chromophores: binding specificity and photochemistry.

Authors:  Stephanie Pröll; Brigitte Wilhelm; Bruno Robert; Hugo Scheer
Journal:  Biochim Biophys Acta       Date:  2006-05-12

6.  Comparison of low oxidoreduction potential cytochrome c553 from Desulfovibrio vulgaris with the class I cytochrome c family.

Authors:  M J Blackledge; F Guerlesquin; D Marion
Journal:  Proteins       Date:  1996-02

7.  Heme redox potential control in de novo designed four-alpha-helix bundle proteins.

Authors:  J M Shifman; B R Gibney; R E Sharp; P L Dutton
Journal:  Biochemistry       Date:  2000-12-05       Impact factor: 3.162

8.  De novo designed cyclic-peptide heme complexes.

Authors:  Michael M Rosenblatt; Jiangyun Wang; Kenneth S Suslick
Journal:  Proc Natl Acad Sci U S A       Date:  2003-10-31       Impact factor: 11.205

9.  Crystal structure of spinach plastocyanin at 1.7 A resolution.

Authors:  Y Xue; M Okvist; O Hansson; S Young
Journal:  Protein Sci       Date:  1998-10       Impact factor: 6.725

10.  Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides.

Authors:  A J Chirino; E J Lous; M Huber; J P Allen; C C Schenck; M L Paddock; G Feher; D C Rees
Journal:  Biochemistry       Date:  1994-04-19       Impact factor: 3.162

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  1 in total

1.  Design and engineering of water-soluble light-harvesting protein maquettes.

Authors:  Goutham Kodali; Joshua A Mancini; Lee A Solomon; Tatiana V Episova; Nicholas Roach; Christopher J Hobbs; Pawel Wagner; Olga A Mass; Kunche Aravindu; Jonathan E Barnsley; Keith C Gordon; David L Officer; P Leslie Dutton; Christopher C Moser
Journal:  Chem Sci       Date:  2016-08-17       Impact factor: 9.825

  1 in total

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