The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Biological Chemistry of Carbon Monoxide
Abstract
Carbon monoxide (CO) has many effects in biology due to its complex biochemical activities. These actions of CO depend primarily on its ability to bind heme proteins (Hp) and to inhibit or alter their biochemical functions. Whether CO is derived from exogenous or endogenous sources, its cellular activity is related to its concentration and the concentration of molecular O(2), as well as to the availability of reduced transition metals such as Fe(II). In this respect, the CO/O(2) ratio and O(2)-dependent changes in local oxidation-reduction state assume critical importance in determining the physiological effects of CO by affecting the functions of specific Hp. By interacting with Hp, CO influences electron-transport reactions in a variety of ways, which can produce either prooxidant or antioxidant effects. Similarly, Hp relationships also govern how changes in CO concentration influence the physiological and pathological effects of nitric oxide and the relationships of the two biologically active gases to metal-catalyzed oxidations. This article provides a brief update on the biochemistry of CO as it relates to Hp binding, chemical oxidative processes, and cellular function.
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Cites
Choi, A. M., & Alam, J. (1996) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.15.1.8679227 · Cited by 1,126
Oxygen Activation by Cytochrome P-4501
White, R. E., & Coon, M. J. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.001531 · Cited by 1,023 · cited 1×
“They catalyze hydroxylation reactions involving the uptake of a pair of electrons from NADPH with reduction of one atom of O 2 to H 2 O and incorporation of the other into the substrate (109).”
Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5375 · Cited by 782
Mitochondrial oxidative stress after carbon monoxide hypoxia in the rat brain.
Zhang, J., & Piantadosi, C. A. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115980 · Cited by 320
Self-citationKinetic pathways and barriers for ligand binding to myoglobin
Olson, J. S., & Phillips, G. N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17593 · Cited by 259 · cited 2×
“For sperm whale myoglobin, the overall association rate constants for CO, O 2 , and NO are 0.5, 17, and 22 m M s 2 1 , respectively (62).”
Influential
Cited by
The therapeutic potential of carbon monoxide
Motterlini, R., & Otterbein, L. E. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3228 · Cited by 1,638
Carbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications
Wu, L., & Wang, R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.3 · Cited by 962
Fukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005234 · Cited by 389
Zuckerbraun, B. S., Chin, B. Y., Bilban, M., d'Avila, J. D. C., Rao, J., Billiar, T. R., & Otterbein, L. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-6644com · Cited by 323
Carbon monoxide, reactive oxygen signaling, and oxidative stress
Piantadosi, C. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.013 · Cited by 281
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Metadata
- Authors
- Piantadosi, C. A.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2002-04
- Volume
- 4
- Issue
- 2
- Pages
- 259-270
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2056409142
- Cited by
- 201
- References
- 5
- FWCI
- 2.27
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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