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Antioxidants
Volume 10
Issue 6
10.3390/antiox10060946
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Article

Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State

by
Tom E. Forshaw
1,
Julie A. Reisz
1,
Kimberly J. Nelson
2,
Rajesh Gumpena
2,
J. Reed Lawson
2,
Thomas J. Jönsson
2,
Hanzhi Wu
1,
Jill E. Clodfelter
2,
Lynnette C. Johnson
2,
Cristina M. Furdui
1,3,4,* and
W. Todd Lowther
2,3,4,*
1
Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA
2
Center for Structural Biology, Department of Biochemistry, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA
3
Center for Redox Biology and Medicine, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA
4
Comprehensive Cancer Center, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, USA
*
Authors to whom correspondence should be addressed.
Academic Editors: Joris Messens, Daria Ezeriņa and Jesalyn Bolduc
Antioxidants 2021, 10(6), 946; https://doi.org/10.3390/antiox10060946
Received: 11 May 2021 / Revised: 4 June 2021 / Accepted: 8 June 2021 / Published: 11 June 2021
(This article belongs to the Special Issue Redox Language of the Cell)
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Abstract

Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decamers and disulfide-linked dimers, with the hyperoxidized inactive state (-SO2H) favoring the multimeric structure of the reduced enzyme. Here, we present a study on the structural requirements for the repair of hyperoxidized 2-Cys Prxs by human sulfiredoxin (Srx) and the relative efficacy of physiological reductants hydrogen sulfide (H2S) and glutathione (GSH) in this reaction. The crystal structure of the toroidal Prx1-Srx complex shows an extended active site interface. The loss of this interface within engineered Prx2 and Prx3 dimers yielded variants more resistant to hyperoxidation and repair by Srx. Finally, we reveal for the first time Prx isoform-dependent use of and potential cooperation between GSH and H2S in supporting Srx activity. View Full-Text
Keywords: redox; peroxiredoxin; sulfiredoxin; thiols; hydrogen sulfide; glutathione redox; peroxiredoxin; sulfiredoxin; thiols; hydrogen sulfide; glutathione
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MDPI and ACS Style

Forshaw, T.E.; Reisz, J.A.; Nelson, K.J.; Gumpena, R.; Lawson, J.R.; Jönsson, T.J.; Wu, H.; Clodfelter, J.E.; Johnson, L.C.; Furdui, C.M.; Lowther, W.T. Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State. Antioxidants 2021, 10, 946. https://doi.org/10.3390/antiox10060946

AMA Style

Forshaw TE, Reisz JA, Nelson KJ, Gumpena R, Lawson JR, Jönsson TJ, Wu H, Clodfelter JE, Johnson LC, Furdui CM, Lowther WT. Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State. Antioxidants. 2021; 10(6):946. https://doi.org/10.3390/antiox10060946

Chicago/Turabian Style

Forshaw, Tom E., Julie A. Reisz, Kimberly J. Nelson, Rajesh Gumpena, J. Reed Lawson, Thomas J. Jönsson, Hanzhi Wu, Jill E. Clodfelter, Lynnette C. Johnson, Cristina M. Furdui, and W. Todd Lowther. 2021. "Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State" Antioxidants 10, no. 6: 946. https://doi.org/10.3390/antiox10060946

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