Cited by 281Heme Oxygenase-1 and Carbon MonoxideHemoglobin structure and functionRedox biology and oxidative stress

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Carbon monoxide, reactive oxygen signaling, and oxidative stress

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Piantadosi, Claude A.·2008·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2008.05.013PMC PMC2570053

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Abstract

The ubiquitous gas, carbon monoxide (CO), is of substantial biological importance, but apart from its affinity for reduced transition metals, particularly heme-iron, it is surprisingly nonreactive-as is the ferrous-carbonyl-in living systems. CO does form strong complexes with heme proteins for which molecular O2 is the preferred ligand and to which are attributed diverse physiological, adaptive, and toxic effects. Lately, it has become apparent that both exogenous and endogenous CO produced by heme oxygenase engender a prooxidant milieu in aerobic mammalian cells which initiates signaling related to reactive oxygen species (ROS) generation. ROS signaling contingent on CO can be segregated by CO concentration-time effects on cellular function, by the location of heme proteins, e.g., mitochondrial or nonmitochondrial sites, or by specific oxidation-reduction (redox) reactions. The fundamental responses to CO involve overt physiological regulatory events, such as activation of redox-sensitive transcription factors or stress-activated kinases, which institute compensatory expression of antioxidant enzymes and other adaptations to oxidative stress. In contrast, responses originating from highly elevated or protracted CO exposures tend to be nonspecific, produce untoward biological oxidations, and interfere with homeostasis. This brief overview provides a conceptual framework for understanding CO biology in terms of this physiological-pathological hierarchy.

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Self-citation

Authors: Piantadosi, C. A.
Affiliations: Duke University (US)
Corresponding author: Piantadosi, Claude A.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2008-09
Volume: 45
Issue: 5
Pages: 562-569
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2008.05.013
PMC: PMC2570053
OpenAlex: W2087826558
Cited by: 281
References: 145
Citations by year: 2026: 11 · 2025: 10 · 2024: 15 · 2023: 13 · 2022: 19 · 2021: 16 · 2020: 21 · 2019: 8 · 2018: 16 · 2017: 13 · 2016: 7 · 2015: 11 · 2014: 17 · 2013: 16 · 2012: 16
FWCI: 1.83
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Heart, Lung, and Blood Institute (R01HL090679)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: carbon monoxide, reactive oxygen species, oxidative stress, heme proteins, heme oxygenase, pro-oxidant activity, redox signaling, stress-activated kinases, redox-sensitive transcription factors, antioxidant enzymes, co-toxicity
MeSH terms: Adaptation, Biological, Animals, Carbon Monoxide, Hemeproteins, Humans, Signal Transduction, Reactive Oxygen Species, Oxidative Stress

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Carbon monoxide, reactive oxygen signaling, and oxidative stress

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