Electron Paramagnetic Resonance Investigation of Nitrite Binding in Myoglobin Article Swipe
It has been proposed that myoglobin (Mb) may act as a nitrite reductase under hypoxic conditions. Any mechanism describing such activity should take into account the binding geometry of the ligand to the heme. Crystal structures of horse-heart Mb and human hemoglobin-nitrite complexes suggest that the anion adopts an uncommon O -nitrito binding mode. Electron Paramagnetic Resonance (EPR) spectroscopy was employed to investigate the nature of nitrite binding to Mb at pH values ranging from 6.5 to 10.8. Results suggest that for ferric Mb at low pH, nitrite binds in the O -bound nitrito mode resulting in a low-spin (LS) iron center. Further a high-spin (HS) iron center is observed at high pH in Mb-Nitrite with spectral values different to that of purely HS-Mb that is proposed to be due to an N- bound nitrite. The yields of these two species were found to be influenced by pH. Background Myoglobin has been theorized to have a role as a nitrite reductase. Results O -bound nitrite produces a low-spin ferric heme complex, whilst at high pH a high-spin species is found proposed to be the N -bound form. Conclusion Nitrite may bind to heme in myoglobin via N-nitro or O-nitrito mode. Significance The mechanism of any nitrite reduction will depend on its binding to the heme cofactor.
Related Topics
Concepts
Myoglobin
Nitrite
Chemistry
Heme
Electron paramagnetic resonance
Nitrite reductase
Ferric
Methemoglobin
Cofactor
Ligand (biochemistry)
Hemeprotein
Metalloprotein
Hemoglobin
Electron transfer
Inorganic chemistry
Resonance Raman spectroscopy
Crystallography
Photochemistry
Nuclear magnetic resonance
Biochemistry
Enzyme
Raman spectroscopy
Organic chemistry
Nitrate
Receptor
Optics
Physics
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/252775
- https://www.biorxiv.org/content/biorxiv/early/2018/01/24/252775.full.pdf
- OA Status
- green
- Cited By
- 2
- References
- 30
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2790149231
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W2790149231Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1101/252775Digital Object Identifier
- Title
-
Electron Paramagnetic Resonance Investigation of Nitrite Binding in MyoglobinWork title
- Type
-
preprintOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2018Year of publication
- Publication date
-
2018-01-24Full publication date if available
- Authors
-
Matt Bawn, Fraser MacMillanList of authors in order
- Landing page
-
https://doi.org/10.1101/252775Publisher landing page
- PDF URL
-
https://www.biorxiv.org/content/biorxiv/early/2018/01/24/252775.full.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
-
https://www.biorxiv.org/content/biorxiv/early/2018/01/24/252775.full.pdfDirect OA link when available
- Concepts
-
Myoglobin, Nitrite, Chemistry, Heme, Electron paramagnetic resonance, Nitrite reductase, Ferric, Methemoglobin, Cofactor, Ligand (biochemistry), Hemeprotein, Metalloprotein, Hemoglobin, Electron transfer, Inorganic chemistry, Resonance Raman spectroscopy, Crystallography, Photochemistry, Nuclear magnetic resonance, Biochemistry, Enzyme, Raman spectroscopy, Organic chemistry, Nitrate, Receptor, Optics, PhysicsTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
2Total citation count in OpenAlex
- Citations by year (recent)
-
2024: 1, 2018: 1Per-year citation counts (last 5 years)
- References (count)
-
30Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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