Glass matrix-facilitated thermal reduction: a tool for probing reactions of met hemoglobin with nitrite and nitric oxide
Open accessAbstract
Isolating elemental steps that comprise a protein reaction in solution is a difficult process. In this study, the use of sugar-derived glass matrices is evaluated as a biophysical tool to help dissect out elemental steps and isolate intermediates. Two features of the glass are utilized in this endeavor: (i) the capacity of trehalose glass matrices to support thermal reduction over macroscopic distances; and (ii) the ability of glass matrices to significantly damp large amplitude protein dynamics. The focus of the study is on the reaction of nitric oxide (NO) with a nitrite ion coordinated to the heme iron of hemoglobin (Hb). The thermal reduction property of the glass is used to generate NO from nitrite within the glass, and the damping of protein dynamics is used to control entry of NO into the distal heme pocket of Hb, where it can either interact with bound nitrite or bind to the heme iron. The results not only relate to earlier controversial studies addressing the reactions of Hb with NO and nitrite but also raise the prospect that these properties of sugar-derived glassy matrices can be exploited as a new biophysical tool to modulate and probe reactions of NO with hemeproteins as well as a wide range of other metalloproteins.
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Several proposed mechanisms explain how nitrite-derived bioactivity can be exported from the red blood cell, generally involving either a compartment model with submembrane localization or formation of another nitrogen oxide such as a nitrosothiol or N2O3.
“Several proposed mechanisms have been constructed to explain how nitrite-derived bioactivity can be exported from the red blood cell and these generally involve either a compartment model with submembrane localization of the reaction allowing for inefficient free NO escape, or the formation of another nitrogen oxide such as a nitrosothiol or N2O3 that can get out of the red blood cell and carry NO”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [52]
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Mechanisms of nitrite bioactivation
Kim-Shapiro, D. B., & Gladwin, M. T. (2014) · Nitric Oxide · doi:10.1016/j.niox.2013.11.002 · Cited by 157 · see citing works
- Authors
- Navati, M. S., & Friedman, J. M.
- Affiliations
- Albert Einstein College of Medicine (US)
- Corresponding author
- Friedman, Joel M.
- ORCID
- Friedman, Joel M.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-02-10
- Volume
- 114
- Issue
- 8
- Pages
- 2938-2943
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- PMC
- PMC2858684
- OpenAlex
- W2007166146
- Cited by
- 12
- References
- 30
- Citations by year
- 2016: 2 · 2015: 2 · 2014: 1 · 2013: 4 · 2012: 1
- FWCI
- 0.98
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journal of Physical Chemistry B (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p01hl071064-05)
- National Heart, Lung, and Blood Institute (P01HL-071064)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Physical Sciences › Materials Science › Ceramics and Composites › Glass properties and applications
- Keywords
- methemoglobin, nitric oxide, nitrite, thermal reduction, heme iron, distal heme pocket, reaction intermediates
- MeSH terms
- Glass, Methemoglobin, Nitric Oxide, Nitrites, Oxidation-Reduction, Temperature, Protein Folding
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