Nitrite coordination in myoglobin.
Abstract: The coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional theory (DFT) calculations. The DFT Natural Bond Orbital (NBO) analysis and the extensive isotope-labeling in the resonance Raman experiments indicate that NO (O1NO2) is bound to the heme Fe via O1. Based on the vibrational characterization of the reversible transition between low and high spin FeONO/2-nitrovinyl species, we suggest that the key step that triggers the spin-change is the increase of the proximal FeN bond length. The frequencies of the O and N sensitive bands of the FeONO/2-nitrovinyl species remained largely unchanged in the low- to high-spin transition. Therefore the "greening" process in the reaction of ferric Mb with NO proceeds through the FeONO/2-nitrovinyl species, which can exist in either the high or low-spin state.
Copyright © 2016 Elsevier Inc. All rights reserved.
Publication Date: 2016-10-14 PubMed ID: 27815981DOI: 10.1016/j.jinorgbio.2016.10.002Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research outlines a study of the configuration of nitrite in myoglobin, specifically concentrating on how nitrite is bound to heme iron and 2-vinyl, using resonance Raman spectroscopy and density functional theory (DFT) calculations.
Nitrite Coordination in Myoglobin
The study pertains to the analysis of how nitrite gets coordinated in myoglobin (Mb), a protein in muscle cells that carries and stores oxygen. Mainly, this research revolves around understanding the computational and spectroscopic characterization of this coordination.
- Resonance Raman spectroscopy and Density Functional Theory (DFT) calculations: These two methods have been employed to identify and compute the frequencies of nitrite when it is bound to heme iron and 2-vinyl in myoglobin. Raman spectroscopy is a spectroscopic technique used to observe vibrational, rotational, and other low-frequency modes in a system, while DFT calculations allow for the study of the electronic structure of multi-electron systems.
Key Findings
- Finding the Nitric Oxide (NO) binding: The study uses DFT Natural Bond Orbital (NBO) analysis and extensive isotope-labelling in the resonance Raman experiments to conclude that NO (O1NO2) is bound to the heme Fe via Oxygen atom O1.
- Spin Transition: The research also studies the vibrational characterization of the transition between low and high spin FeONO/2-nitrovinyl species. The key step that triggers the change in spin is found to be the increase of the proximal (closest to the iron atom) FeN bond length.
- Greening Process: The study suggests that the ‘greening’ process – a color change observed in the reaction of ferric myoglobin (FeMb) with nitric oxide (NO), happens via the FeONO/2-nitrovinyl species, which can be in either the high or low-spin state. Importantly, the frequencies of the oxygen and nitrogen-sensitive bands of these species remained largely unchanged in the transition from low to high spin.
Implication of the Research
This study adds value to the scientific understanding of the coordination of nitrites in myoglobin and contributes to the broader research of protein function and behavior. The research findings can potentially provide insights on how oxygen is stored and carried within muscles, shedding more light on the biochemistry of muscle tissues.
Cite This Article
APA
Ioannou A, Lambrou A, Daskalakis V, Pinakoulaki E.
(2016).
Nitrite coordination in myoglobin.
J Inorg Biochem, 166, 49-54.
https://doi.org/10.1016/j.jinorgbio.2016.10.002 Publication
Researcher Affiliations
- Department of Chemistry, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus.
- Department of Chemistry, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus.
- Department of Environmental Science and Technology, Cyprus University of Technology, 3603 Lemessos, Cyprus.
- Department of Chemistry, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus. Electronic address: effiep@ucy.ac.cy.
MeSH Terms
- Animals
- Heme / chemistry
- Horses
- Iron / chemistry
- Myoglobin / chemistry
- Nitrites / chemistry
Citations
This article has been cited 3 times.- Valianti VK, Tselios C, Pinakoulaki E. Reversible thermally induced spin crossover in the myoglobin-nitrito adduct directly monitored by resonance Raman spectroscopy.. RSC Adv 2023 Mar 14;13(13):9020-9025.
- De Backer J, Razzokov J, Hammerschmid D, Mensch C, Hafideddine Z, Kumar N, van Raemdonck G, Yusupov M, Van Doorslaer S, Johannessen C, Sobott F, Bogaerts A, Dewilde S. The effect of reactive oxygen and nitrogen species on the structure of cytoglobin: A potential tumor suppressor.. Redox Biol 2018 Oct;19:1-10.
- Nilsson ZN, Mandella BL, Sen K, Kekilli D, Hough MA, Moënne-Loccoz P, Strange RW, Andrew CR. Distinguishing Nitro vs Nitrito Coordination in Cytochrome c' Using Vibrational Spectroscopy and Density Functional Theory.. Inorg Chem 2017 Nov 6;56(21):13205-13213.
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