skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Redox-dependent Structural Changes in Archaeal and Bacterial Rieske-type [2Fe-2S] Clusters

Abstract

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 {angstrom} 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.

Authors:
Publication Date:
Research Org.:
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Org.:
USDOE Office of Science (US)
OSTI Identifier:
815847
Report Number(s):
SLAC-REPRINT-2002-252
TRN: US200319%%551
DOE Contract Number:  
AC03-76SF00515
Resource Type:
Journal Article
Journal Name:
Protein Science
Additional Journal Information:
Other Information: Protein Sci.11:2969,2002; PBD: 1 Jan 2002
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ABSORPTION; AVAILABILITY; BOND LENGTHS; ELECTRON TRANSFER; ELECTRONS; FERREDOXIN; OXYGENASES; PROTEINS; STRAINS; TRANSFORMATIONS; STANFORD SYNCHROTRON RADIATION LABORATORY

Citation Formats

Cosper, N J. Redox-dependent Structural Changes in Archaeal and Bacterial Rieske-type [2Fe-2S] Clusters. United States: N. p., 2002. Web. doi:10.1110/ps.0222402.
Cosper, N J. Redox-dependent Structural Changes in Archaeal and Bacterial Rieske-type [2Fe-2S] Clusters. United States. https://doi.org/10.1110/ps.0222402
Cosper, N J. 2002. "Redox-dependent Structural Changes in Archaeal and Bacterial Rieske-type [2Fe-2S] Clusters". United States. https://doi.org/10.1110/ps.0222402.
@article{osti_815847,
title = {Redox-dependent Structural Changes in Archaeal and Bacterial Rieske-type [2Fe-2S] Clusters},
author = {Cosper, N J},
abstractNote = {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 {angstrom} 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.},
doi = {10.1110/ps.0222402},
url = {https://www.osti.gov/biblio/815847}, journal = {Protein Science},
number = ,
volume = ,
place = {United States},
year = {Tue Jan 01 00:00:00 EST 2002},
month = {Tue Jan 01 00:00:00 EST 2002}
}