Abstract
The heat shock protein 70 (HSP70) in the chloroplast of Chlamydomonas reinhardtii, termed HSP70B, interacts with chloroplast-targeted DnaJ-like proteins (CDJs). In this work we focus on two CDJ co-chaperones (CDJ3 and CDJ4) of HSP70B which contain a redox-active Fe-S cluster (Dorn et al. Biochem. J. 427, 205 [2010]). We have performed Mössbauer spectroscopy on 57Fe enriched CDJ3 an) CDJ4. Our results indicate that both proteins have unusual [4Fe4S] 2+ clusters showing structural inhomogeneity of the two [Fe 2.5+-Fe 2.5+] pairs. The spectra have been analyzed by means of two components with δ-values characteristic for Fe 2.5+ centers, but the differences in ΔE Q indicate variations in their tetrahedral coordination spheres.
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Acknowledgements
This work has been supported by the research initiative NANOKAT and by the DFG (SPP 1927 “Iron-Sulfur for Life”, project Schu 1271/17-1 and SFB/TRR175, project C02).
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This article is part of the Topical Collection on Proceedings of the International Conference on the Applications of the Mössbauer Effect (ICAME 2017), Saint-Petersburg, Russia, 3-8 September 2017
Edited by Valentin Semenov
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Auerbach, H., Kalienkova, V., Schroda, M. et al. Mössbauer spectroscopy of the chloroplast-targeted DnaJ-like proteins CDJ3 and CDJ4. Hyperfine Interact 238, 86 (2017). https://doi.org/10.1007/s10751-017-1458-y
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DOI: https://doi.org/10.1007/s10751-017-1458-y