Literature DB >> 12613610

Engineering redox functions in a nucleic acid binding protein.

Jon R Wilson1, Daren J Caruana, Gianfranco Gilardi.   

Abstract

A nucleic acid binding protein, rop, has conserved topology with a number of redox proteins; this is exploited to engineer haem binding, expanding its function as a redox protein.

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Year:  2003        PMID： 12613610     DOI： 10.1039/b209443f

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  5 in total

1.  Modulation of function in a minimalist heme-binding membrane protein.

Authors:  Sandip Shinde; Jeanine M Cordova; Brian W Woodrum; Giovanna Ghirlanda
Journal:  J Biol Inorg Chem       Date:  2012-02-04       Impact factor: 3.358

2.  Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins.

Authors:  Shona C Patel; Luke H Bradley; Sayuri P Jinadasa; Michael H Hecht
Journal:  Protein Sci       Date:  2009-07       Impact factor: 6.725

Review 3.  Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.

Authors:  Jing Liu; Saumen Chakraborty; Parisa Hosseinzadeh; Yang Yu; Shiliang Tian; Igor Petrik; Ambika Bhagi; Yi Lu
Journal:  Chem Rev       Date:  2014-04-23       Impact factor: 60.622

Review 4.  Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.

Authors:  Parisa Hosseinzadeh; Yi Lu
Journal:  Biochim Biophys Acta       Date:  2015-08-21

5.  Engineering heme binding sites in monomeric rop.

Authors:  Giovanna Di Nardo; Almerinda Di Venere; Giampiero Mei; Sheila J Sadeghi; Jon R Wilson; Gianfranco Gilardi
Journal:  J Biol Inorg Chem       Date:  2009-01-17       Impact factor: 3.358
  5 in total

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