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Science 19 January 2007:
Vol. 315. no. 5810, pp. 387 - 389
DOI: 10.1126/science.1133114
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Reports

High-Throughput Identification of Catalytic Redox-Active Cysteine Residues

Dmitri E. Fomenko,1 Weibing Xing,2 Blakely M. Adair,3 David J. Thomas,3 Vadim N. Gladyshev1*

Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases. This method is independent of protein family, structure, and taxon. We used it to selectively detect the majority of known proteins with redox-active Cys and to make additional predictions, one of which was verified. Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins.

1 Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.
2 Curriculum in Toxicology, University of North Carolina, Chapel Hill, NC 27599, USA.
3 Experimental Toxicology Division, National Health and Environmental Effects Research Laboratory, U.S. Environmental Protection Agency, Research Triangle Park, NC 27709, USA.

* To whom correspondence should be addressed. E-mail: vgladyshev1{at}unl.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)