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Cited by 84Redox biology and oxidative stressHemoglobin structure and functionMetal-Catalyzed Oxygenation Mechanisms

Cytochrome c: a catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration

Castro, Laura, Eiserich, Jason P., Sweeney, Scott, Radi, Rafael, Freeman, Bruce A.·2004·Archives of Biochemistry and Biophysics
DOI 10.1016/j.abb.2003.08.033
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Abstract

Nitration of protein tyrosine residues to 3-nitrotyrosine (NO2Tyr) serves as both a marker and mediator of pathogenic reactions of nitric oxide (*NO), with peroxynitrite (ONOO-) and leukocyte peroxidase-derived nitrogen dioxide (*NO2) being proximal mediators of nitration reactions in vivo. Cytochrome c is a respiratory and apoptotic signaling heme protein localized exofacially on the inner mitochondrial membrane. We report herein a novel function for cytochrome c as a catalyst for nitrite (NO2-) and hydrogen peroxide (H2O2)-mediated nitration reactions. Cytochrome c catalyzes both self- and adjacent-molecule (hydroxyphenylacetic acid, Mn-superoxide dismutase) nitration via heme-dependent mechanisms involving tyrosyl radical and *NO2 production, as for phagocyte peroxidases. Although low molecular weight phenolic nitration yields were similar for cytochrome c and the proteolytic fragment of cytochrome c microperoxidase-11 (MPx-11), greater extents of protein nitration occurred when MPx-11 served as catalyst. Partial proteolysis of cytochrome c increased both the peroxidase and nitrating activities of cytochrome c. Extensive tyrosine nitration of Mn-superoxide dismutase occurred when exposed to either cytochrome c or MPx-11 in the presence of H2O2 and NO2-, with no apparent decrease in catalytic activity. These results reveal a post-translational tyrosine modification mechanism that is mediated by an abundant hemoprotein present in both mitochondrial and cytosolic compartments. The data also infer that the distribution of specific proteins capable of serving as potent catalysts of nitration can lend both spatial and molecular specificity to biomolecule nitration reactions.

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  • Protein nitration can also occur through the reaction of nitrite with heme proteins in the presence of hydrogen peroxide.

    “Importantly, protein nitration can also occur through the reaction of nitrite with heme proteins in the presence of hydrogen peroxide (153, 154).”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [154]

  • Generation of nitrogen dioxide and subsequent protein nitration from nitrite oxidation by peroxidases and other heme proteins was appreciated many years before the biologic potential for nitrite reduction to NO was realized.

    “Generation of nitrogen dioxide and subsequent protein nitration from nitrite oxidation by peroxidases such as myeloperoxidase[108], eosinophil peroxidase [109] and also other heme proteins such as cytochrome c [110], hemoglobin [111, 112] and myoglobin [112, 113] was appreciated many years before the biologic potential for nitrite-reduction to NO was realized.”

    From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [110]

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Authors
Castro, L., Eiserich, J. P., Sweeney, S., Radi, R., & Freeman, B. A.
Affiliations
  • Universidad de la República de Uruguay (UY)
  • University of Alabama at Birmingham (US)
Corresponding author
Castro, Laura
ORCID
Castro, Laura
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2004-01
Volume
421
Issue
1
Pages
99-107
ISSN
0003-9861 (ISSN-L)
DOI
10.1016/j.abb.2003.08.033
OpenAlex
W2010106046
Cited by
84
References
63
Citations by year
2024: 2 · 2021: 1 · 2020: 1 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 1 · 2015: 4 · 2014: 5 · 2013: 2 · 2012: 5
FWCI
2.07
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Archives of Biochemistry and Biophysics (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
cytochrome c, protein nitration, nitrotyrosine, nitrite, hydrogen peroxide, peroxynitrite, nitric oxide, tyrosyl radical, microperoxidase-11, Mn superoxide dismutase, post-translational modification, tyrosine nitration, leukocyte peroxidase, mitochondrial proteins
MeSH terms
Animals, Catalysis, Cattle, Horses, Humans, Hydrogen Peroxide, Mitochondria, Liver, Peroxidase, Myocardium, Nitrates, Nitrites, Phenylacetates, Recombinant Proteins, Serum Albumin, Bovine, Superoxide Dismutase, Tyrosine, Jurkat Cells, Cytochromes c, Rats

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