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FOR THE RECORD

Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters

¹ Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602, USA
² Department of Biochemistry and Molecular Biology, Nippon Medical School, Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan
³ Department of Bioengineering, Soka University, Hachioji, Tokyo 192-8577, Japan

Reprint requests to: Nathaniel J. Cosper, Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA; e-mail: ncosper{at}uga.edu; fax: (706) 542-9454.

Proteins containing Rieske-type [2Fe-2S] clusters play important roles in many biological electron transfer reactions. Typically, [2Fe-2S] clusters are not directly involved in the catalytic transformation of substrate, but rather supply electrons to the active site. We report herein X-ray absorption spectroscopic (XAS) data that directly demonstrate an average increase in the iron–histidine bond length of at least 0.1 Å upon reduction of two distantly related Rieske-type clusters in archaeal Rieske ferredoxin from Sulfolobus solfataricus strain P-1 and bacterial anthranilate dioxygenases from Acinetobacter sp. strain ADP1. This localized redox-dependent structural change may fine tune the protein–protein interaction (in the case of ARF) or the interdomain interaction (in AntDO) to facilitate rapid electron transfer between a lower potential Rieske-type cluster and its redox partners, thereby regulating overall oxygenase reactions in the cells.

Keywords: Anthranilate dioxygenase (AntDO); archaeal Rieske ferredoxin (ARF); iron-sulfur cluster; reduction potential; Rieske-type ferredoxin; X-ray absorption fine structure; X-ray absorption spectroscopy

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