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Cited by 510Hemoglobin structure and functionNitric Oxide and Endothelin EffectsMetal-Catalyzed Oxygenation Mechanisms

Nitric oxide and iron proteins

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Cooper, Chris E.·1999·Biochimica et Biophysica Acta (BBA) - Bioenergetics
DOI 10.1016/s0005-2728(99)00021-3
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Abstract

Nitric oxide interactions with iron are the most important biological reactions in which NO participates. Reversible binding to ferrous haem iron is responsible for the observed activation of guanylate cyclase and inhibition of cytochrome oxidase. Unlike carbon monoxide or oxygen, NO can also bind reversibly to ferric iron. The latter reaction is responsible for the inhibition of catalase by NO. NO reacts with the oxygen adduct of ferrous haem proteins (e.g. oxyhaemoglobin) to generate nitrate and ferric haem; this reaction is responsible for the majority of NO metabolism in the vasculature. NO can also interact with iron-sulphur enzymes (e.g. aconitase, NADH dehydrogenase). This review describes the underlying kinetics, thermodynamics, mechanisms and biological role of the interactions of NO with iron species (protein and non-protein bound). The possible significance of iron reactions with reactive NO metabolites, in particular peroxynitrite and nitroxyl anion, is also discussed.

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  • Competing reactions, namely NO scavenging by ferrous heme and NO dioxygenation, greatly decrease the amount of bioavailable NO generated by reactions of nitrite with heme proteins.

    “It should be noted that competing reactions, namely the scavenging of NO by the ferrous heme [rate constants in the order of 1.7 × 107 to 1.5 × 108 M−1s−1 (180, 967), Eq. 6] and the rate of NO dioxygenation [rate constants in the order of 3.4 × 107 to 8.9 × 107 M−1s−1 for mammalian Hb/Mb (264, 341), Eq. 8] greatly decrease the amount of bioavailable NO generated by the reactions of nitrite with he”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [180]

  • Nitrosylation of nonheme iron sites in aconitase and prolyl hydroxylase inhibits these enzymes and can regulate metabolism and low-oxygen responses.

    “Nitrosylation of the nonheme iron sites in aconitase [238] and prolyl hydroxylase [247] also lead to enzyme inhibition and thus can serve a regulatory role that impacts metabolism and response to low oxygen levels.”

    From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [238]

  • Nonheme iron complexes generally have slower NO on rates (10^3-10^6) than heme systems (>10^7).

    “With respect to coordination of NO, nonheme iron complexes tend to have slower on rates 103-106 [238] than heme systems (>107; [11]).”

    From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [238]

  • Prolyl hydroxylases are classic nonheme iron complexes involved in collagen formation and HIF-1α stabilization.

    “Another classic example that highlights the diversity and importance of nonheme iron complexes in metabolism [235, 236] is the prolyl hydroxylases, which are involved in collagen formation and stabilization of HIF-1α [237-239].”

    From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [238]

  • Nonheme iron may be at a crossroads for forming intermediates such as NO, NO2 or RSNO, thereby directing the redox signaling landscape.

    “Nonheme iron may be at the crossroads for formation of intermediates that lead to species like, NO, NO2 or RSNO, thus directing/changing the redox signaling landscape [238, 240].”

    From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [238]

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Research works printed but not linked: 4

  1. G.B. Richter-Addo, P. Legzdins, Metal Nitrosyls, Oxford University Press, New York, 1992.
  2. M. Lepoivre, P. Bobe, Y. Henry, Reversible alteration of ribonucleotide reductase EPR properties in tumor target cells co-cultured with macrophages producing nitric oxide, in: S. Moncada, M. Feelisch, R. Busse, E.A. Higgs (Eds.), Biology of Nitric Oxide, Portland Press, London, 1994, pp. 186^189.
  3. Y.A. Henry, D.J. Singel, Metal^nitrosyl interactions in nitric oxide biology probed by electron paramagnetic resonance spectroscopy, in: M. Feelisch, J.S. Stamler (Eds.), Methods in Nitric Oxide Research, John Wiley, Chichester, 1996, pp. 357^372.
  4. D.J. Singel, J.R.J. Lancaster, Electron paramagnetic reso- nance spectroscopy and nitric oxide biology, in: M. Feelisch, J.S. Stamler (Eds.), Methods in Nitric Oxide Research, John Wiley, Chichester, 1996, pp. 341^356.

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Authors
Cooper, C. E.
Affiliations
University of Essex (GB)
Corresponding author
Cooper, Chris E.
ORCID
Cooper, Chris E.
Venue
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher
Elsevier BV
Published
1999-05
Volume
1411
Issue
2-3
Pages
290-309
ISSN
0005-2728 (ISSN-L)
DOI
10.1016/s0005-2728(99)00021-3
OpenAlex
W2127475487
Cited by
510
References
132
Citations by year
2026: 3 · 2025: 7 · 2024: 12 · 2023: 14 · 2022: 19 · 2021: 17 · 2020: 12 · 2019: 20 · 2018: 15 · 2017: 18 · 2016: 15 · 2015: 21 · 2014: 18 · 2013: 11 · 2012: 17
FWCI
7.06
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
  • PubMed (publishedVersion)
Funders
University of Essex
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
nitric oxide, iron-containing proteins, haem iron, guanylate cyclase activation, cytochrome c oxidase inhibition, catalase inhibition, oxyhemoglobin, nitrate formation, aconitase, NADH dehydrogenase, peroxynitrite, nitroxyl, vascular system, reaction kinetics, thermodynamics
MeSH terms
Animals, Carbon Monoxide, Ferric Compounds, Ferrous Compounds, Hemeproteins, Humans, Iron, Iron-Sulfur Proteins, Kinetics, Models, Chemical, Nitric Oxide, Oxygen, Thermodynamics, Nonheme Iron Proteins

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