Literature DB >> 15554622

Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.

Mark J Ellis1, Svetlana V Antonyuk, Richard W Strange, Gary Sawers, Robert R Eady, S Samar Hasnain.   

Abstract

Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.

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Year:  2004        PMID: 15554622     DOI: 10.1021/ic048966p

Source DB:  PubMed          Journal:  Inorg Chem        ISSN: 0020-1669            Impact factor:   5.165


  3 in total

1.  The structure of the Met144Leu mutant of copper nitrite reductase from Alcaligenes xylosoxidans provides the first glimpse of a protein-protein complex with azurin II.

Authors:  Konstantinos Paraskevopoulos; Michael A Hough; R Gary Sawers; Robert R Eady; S Samar Hasnain
Journal:  J Biol Inorg Chem       Date:  2007-05-15       Impact factor: 3.358

2.  Thermal stability effects of removing the type-2 copper ligand His306 at the interface of nitrite reductase subunits.

Authors:  Andrea Stirpe; Luigi Sportelli; Hein Wijma; Martin Ph Verbeet; Rita Guzzi
Journal:  Eur Biophys J       Date:  2007-03-16       Impact factor: 1.733

3.  The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.

Authors:  Madhuri Chattopadhyay; Eric D Walter; Dustin J Newell; Pilgrim J Jackson; Eliah Aronoff-Spencer; Jack Peisach; Gary J Gerfen; Brian Bennett; William E Antholine; Glenn L Millhauser
Journal:  J Am Chem Soc       Date:  2005-09-14       Impact factor: 15.419

  3 in total

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