Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): A HYSCORE investigation

Weixue Wang; Jikun Li; Ke Wang; Tatyana I. Smirnova; Eric Oldfield

doi:10.1021/ja2008455

Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): A HYSCORE investigation

Weixue Wang, Jikun Li, Ke Wang, Tatyana I. Smirnova, Eric Oldfield

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

IspH is a 4Fe-4S protein that carries out an essential reduction step in isoprenoid biosynthesis. Using hyperfine sublevel correlation (HYSCORE) spectroscopy, we show that pyridine inhibitors of IspH directly bind to the unique fourth Fe in the 4Fe-4S cluster, opening up new routes to inhibitor design, of interest in the context of both anti-bacterial as well as anti-malarial drug discovery.

Original language	English (US)
Pages (from-to)	6525-6528
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	133
Issue number	17
DOIs	https://doi.org/10.1021/ja2008455
State	Published - May 4 2011

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja2008455

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AU - Wang, Ke

AU - Smirnova, Tatyana I.

AU - Oldfield, Eric

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AB - IspH is a 4Fe-4S protein that carries out an essential reduction step in isoprenoid biosynthesis. Using hyperfine sublevel correlation (HYSCORE) spectroscopy, we show that pyridine inhibitors of IspH directly bind to the unique fourth Fe in the 4Fe-4S cluster, opening up new routes to inhibitor design, of interest in the context of both anti-bacterial as well as anti-malarial drug discovery.

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Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): A HYSCORE investigation

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