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

By Nathaniel J. Cosper, D. Matthew Eby, Asako Kounosu, Norio Kurosawa, Ellen L. Neidle, Donald M. Kurtz, Toshio Iwasaki and Robert A. Scott


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

Topics: For the Record
Publisher: Cold Spring Harbor Laboratory Press
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Provided by: PubMed Central
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