Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy-Reference-Cited by-同舟云学术

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Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy

Published:2021-11-03 Issue: Volume: Page:
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:The FEBS Journal

Author:

Hofbauer Stefan¹^ORCID,Pignataro Marcello²^ORCID,Borsari Marco²^ORCID,Bortolotti Carlo Augusto³^ORCID,Di Rocco Giulia³^ORCID,Ravenscroft Gianina⁴⁵^ORCID,Furtmüller Paul G.¹^ORCID,Obinger Christian¹^ORCID,Sola Marco³^ORCID,Battistuzzi Gianantonio²^ORCID

Affiliation:

1. Department of Chemistry Institute of Biochemistry University of Natural Resources and Life Sciences Vienna Austria

2. Department of Chemical and Geological Sciences University of Modena and Reggio Emilia Italy

3. Department of Life Sciences University of Modena and Reggio Emilia Italy

4. Harry Perkins Institute of Medical Research Nedlands WA Australia

5. School of Biomedical Sciences University of Western Australia Nedlands WA Australia

Funder

Università Degli Studi di Modena e Reggio Emila

Austrian Science Fund

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16235

Reference68 articles.

1. Myoglobin: an essential hemoprotein in striated muscle

2. Role of myoglobin in the antioxidant defense of the heart

3. Myoglobin as a versatile peroxidase: Implications for a more important role for vertebrate striated muscle in antioxidant defense

4. Redox Reactions of Myoglobin

5. Reactive nitrogen species generated by heme proteins: Mechanism of formation and targets

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1. Hydrogen peroxide induces heme degradation and protein aggregation in human neuroglobin: roles of the disulfide bridge and hydrogen‐bonding in the distal heme cavity;The FEBS Journal;2022-07-31

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