"tRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme diiron monooxygenase."

Mathevon C, Pierrel F, Oddou JL, Garcia-Serres R, Blondin G, Latour JM, Menage S, Gambarelli S, Fontecave M, Atta M



Published 2007-08-14 in Proc Natl Acad Sci U S A volume 104 .

Pubmed ID: 17679698
DOI identifier: -

Abstract:
MiaE catalyzes the posttranscriptional allylic hydroxylation of 2-methylthio-N-6-isopentenyl adenosine in tRNAs. The Salmonella typhimurium enzyme was heterologously expressed in Escherichia coli. The purified enzyme is a monomer with two iron atoms and displays activity in in vitro assays. The type and properties of the iron center were investigated by using a combination of UV-visible absorption, EPR, HYSCORE, and Mossbauer spectroscopies which demonstrated that the MiaE enzyme contains a nonheme dinuclear iron cluster, similar to that found in the hydroxylase component of methane monooxygenase. This is the first example of an enzyme from this important class of diiron monooxygenases to be involved in the hydroxylation of a biological macromolecule and the second example of a redox metalloenzyme participating in tRNA modification.


This publication refers to following proteins:



Last modification of this entry: Sept. 6, 2012