Cited by 69Hemoglobin structure and functionHeme Oxygenase-1 and Carbon MonoxideMetalloenzymes and iron-sulfur proteins

Nitrite Reductase Activity of Nonsymbiotic Hemoglobins from Arabidopsis thaliana

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Tiso, Mauro, Tejero, Jesús, Kenney, Claire, Frizzell, Sheila, Gladwin, Mark T.·2012·Biochemistry

Abstract

Plant nonsymbiotic hemoglobins possess hexacoordinate heme geometry similar to that of the heme protein neuroglobin. We recently discovered that deoxygenated neuroglobin converts nitrite to nitric oxide (NO), an important signaling molecule involved in many processes in plants. We sought to determine whether Arabidopsis thaliana nonsymbiotic hemoglobins classes 1 and 2 (AHb1 and AHb2, respectively) might function as nitrite reductases. We found that the reaction of nitrite with deoxygenated AHb1 and AHb2 generates NO gas and iron-nitrosyl-hemoglobin species. The bimolecular rate constants for reduction of nitrite to NO are 19.8 ± 3.2 and 4.9 ± 0.2 M(-1) s(-1), respectively, at pH 7.4 and 25 °C. We determined the pH dependence of these bimolecular rate constants and found a linear correlation with the concentration of protons, indicating the requirement for one proton in the reaction. The release of free NO gas during the reaction under anoxic and hypoxic (2% oxygen) conditions was confirmed by chemiluminescence detection. These results demonstrate that deoxygenated AHb1 and AHb2 reduce nitrite to form NO via a mechanism analogous to that observed for hemoglobin, myoglobin, and neuroglobin. Our findings suggest that during severe hypoxia and in the anaerobic plant roots, especially in species submerged in water, nonsymbiotic hemoglobins provide a viable pathway for NO generation via nitrite reduction.

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  1. [36]Sturms R Dispirito AA Hargrove MS 2011 Plant and Cyanobacterial Hemoglobins Reduce Nitrite to Nitric Oxide under Anoxic Conditions Biochemistry 21495624

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Authors
Tiso, M., Tejero, J., Kenney, C., Frizzell, S., & Gladwin, M. T.
Affiliations
  • National Institutes of Health (US)
  • University of Pittsburgh (US)
Corresponding author
  • Tiso, Mauro
  • Gladwin, Mark T.
Venue
Biochemistry
Published
2012-06-20
Volume
51
Issue
26
Pages
5285-5292
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W1979664345
Cited by
69
References
51
Citations by year
2026: 3 · 2025: 2 · 2024: 4 · 2023: 5 · 2021: 4 · 2020: 7 · 2019: 2 · 2018: 5 · 2017: 4 · 2016: 7 · 2015: 7 · 2014: 6 · 2013: 11 · 2012: 2
FWCI
3.94
Type
journal article
Language
en
Open access
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Heart, Lung, and Blood Institute (R01HL096973, P01HL103455, R01HL098032)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
nitrite reductase activity, nitric oxide production, Arabidopsis thaliana, neuroglobin, pH dependence, bimolecular rate constants, hypoxia, submerged plants, chemiluminescence
MeSH terms
Hemoglobins, Hydrogen-Ion Concentration, Nitric Oxide, Nitrite Reductases, Nitrites, Arabidopsis, Arabidopsis Proteins

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