Cited by 589Redox biology and oxidative stressMitochondrial Function and PathologyNitric Oxide and Endothelin Effects

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Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.

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Castro, L, Rodriguez, M, Radi, R·1994·Journal of Biological Chemistry

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Abstract

Mitochondrial and cytosolic aconitases have been indicated as major targets of .NO- and O2-.-mediated toxicity in cells due to the oxidant-mediated disruption of the [4Fe-4S] prosthetic group. However, under circumstances in which both .NO and O2-. are generated, their almost diffusion-controlled combination reaction (k = 6.7 x 10(9) M-1 s-1), leading to the formation of peroxynitrite anion (ONOO-), can out-compete the direct reactions of .NO and O2-. with aconitase and even the enzymatic dismutation of O2-. by superoxide dismutase. In this work, we report that ONOO- reacts with isolated pig heart mitochondrial aconitase at 1.4 x 10(5) M-1 s-1, resulting in a significant loss of enzymatic activity. Aconitase activity was totally recovered after postincubation with thiols and ferrous iron, indicating that ONOO- reactions with the enzyme involve the perturbation of the labile Fe alpha to yield the inactive [3Fe-4S] cluster, which is also evident by spectral changes. On the other hand, anaerobic exposure of isolated aconitase to high concentrations of .NO (> 100 microM) led to a moderate inhibition of the enzyme, which could be fully overcome by .NO displacement under an argon-saturated atmosphere, in agreement with the formation of a reversible inhibitory complex between .NO and the active site of aconitase. Superoxide inactivated mitochondrial aconitase at (3.5 +/- 2) x 10(6) M-1 s-1, a reaction rate 3 orders of magnitude slower than its reaction rate with .NO. O2-. could represent the main mechanism of inactivation of the enzyme in systems in which it is formed without significant concomitant production of .NO. Our results imply that the mechanisms by which .NO and O2-. inactivate aconitase in cell systems may not be simple due to their direct reactions with the iron-sulfur cluster, but may rely on the formation of ONOO-.

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Authors: Castro, L., Rodriguez, M., & Radi, R.
Affiliations: Universidad de la República de Uruguay (UY)
ORCID: Castro, L
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1994-11
Volume: 269
Issue: 47
Pages: 29409-29415
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)43894-x
OpenAlex: W1505685265
Cited by: 589
References: 61
Citations by year: 2026: 2 · 2025: 4 · 2024: 9 · 2023: 5 · 2022: 4 · 2021: 7 · 2020: 5 · 2019: 11 · 2018: 7 · 2017: 9 · 2016: 6 · 2015: 10 · 2014: 15 · 2013: 14 · 2012: 18
FWCI: 15.05
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9475 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Keywords: aconitase, peroxynitrite, nitric oxide, superoxide, iron-sulfur clusters, [4Fe-4S] cluster, enzyme inactivation, mitochondrial aconitase, ferrous iron, oxidative stress
MeSH terms: Aconitate Hydratase, Animals, Iron-Sulfur Proteins, Kinetics, Mitochondria, Heart, Nitrates, Nitric Oxide, Nitroso Compounds, Sulfhydryl Compounds, Swine

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Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.

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