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Reductive nitrosylation of ferric cyanide horse heart myoglobin is limited by cyanide dissociation.
Abstract: Cyanide binds to ferric heme-proteins with a very high affinity, reflecting the very low dissociation rate constant (k(off)). Since no techniques are available to estimate k(off), we report herewith a method to determine k(off) based on the irreversible reductive nitrosylation reaction to trap ferric myoglobin (Mb(III)). The k(off) value for cyanide dissociation from ferric cyanide horse heart myoglobin (Mb(III)-cyanide) was determined at pH 9.2 and 20.0 degrees C. Mixing Mb(III)-cyanide and NO solutions brings about absorption spectral changes reflecting the disappearance of Mb(III)-cyanide with the concomitant formation of ferrous nitrosylated Mb. Since kinetics of reductive nitrosylation of Mb(III) is much faster than Mb(III)-cyanide dissociation, the k(off) value, representing the rate-limiting step, can be directly determined. The k(off) value obtained experimentally matches very well to that calculated from values of the second-order rate constant (k(on)) and of the dissociation equilibrium constant (K) for cyanide binding to Mb(III) (k(off)=k(on)xK).
2010 Elsevier Inc. All rights reserved.
Publication Date: 2010-01-29 PubMed ID: 20116365DOI: 10.1016/j.bbrc.2010.01.092Google Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.
The research article investigates a method to measure cyanide’s dissociation rate constant, k(off), from ferric heme-proteins using ferric myoglobin and the irreversible reductive nitrosylation reaction.
Objective of the Research
- The aim of the research was to establish a technique for estimating the dissociation rate constant (k(off)) of cyanide from ferric heme-proteins. This is crucial as cyanide is known to bind to ferric heme-proteins with high affinity, translating to a very low k(off) value.
Methodology and Experimentation
- The researchers used an irreversible reductive nitrosylation reaction as a means to measure the k(off), focusing primarily on ferric myoglobin (Mb(III)).
- The k(off) for cyanide dissociation from ferric cyanide horse heart myoglobin (Mb(III)-cyanide) was determined at a pH level of 9.2 at a temperature of 20.0 degrees Celsius.
- The researchers introduced nitric oxide (NO) solutions into the Mb(III)-cyanide mix, which led to absorption spectral changes that indicated the disappearance of Mb(III)-cyanide and the formation of ferrous nitrosylated Myoglobin.
Results and Findings
- The research found that the kinetics of reductive nitrosylation of Mb(III) is much quicker than the dissociation of Mb(III)-cyanide. Thus, the k(off) value, which symbolises the rate-limiting step, could be determined directly.
- The experimentally derived k(off) value closely corresponds with the one calculated from the second-order rate constant (k(on)) and the dissociation equilibrium constant (K) for cyanide binding to Mb(III).
Study Implications
- The results of this study can provide valuable insights into the kinetics of cyanide dissociation from ferric heme-proteins and help improve our understanding of these chemical processes. Being able to estimate the k(off) value could also influence the development of better designed strategies aimed at counteracting cyanide poisoning.
Cite This Article
APA
Ascenzi P, di Masi A, Gullotta F, Mattu M, Ciaccio C, Coletta M.
(2010).
Reductive nitrosylation of ferric cyanide horse heart myoglobin is limited by cyanide dissociation.
Biochem Biophys Res Commun, 393(2), 196-200.
https://doi.org/10.1016/j.bbrc.2010.01.092 Publication
Researcher Affiliations
- Department of Biology and Interdepartmental Laboratory for Electron Microscopy, University 'Roma Tre', Roma, Italy. ascenzi@uniroma3.it
MeSH Terms
- Animals
- Ferricyanides / chemistry
- Ferricyanides / metabolism
- Hemoglobins / chemistry
- Hemoglobins / metabolism
- Horses
- Metmyoglobin / chemistry
- Metmyoglobin / metabolism
- Myocardium / metabolism
- Nitric Oxide / metabolism
- Oxidation-Reduction
Citations
This article has been cited 10 times.- Martini MA, Bikbaev K, Pang Y, Lorent C, Wiemann C, Breuer N, Zebger I, DeBeer S, Span I, Bjornsson R, Birrell JA, Rodríguez-Maciá P. Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases. Chem Sci 2023 Mar 15;14(11):2826-2838.
- Hajizadeh S, Bülow L, Ye L. Synthesizing a Hybrid Nanocomposite as an Affinity Adsorbent through Surface-Initiated Atom Transfer Radical Polymerization Catalyzed by Myoglobin. ACS Omega 2021 Apr 20;6(15):10462-10474.
- Dybas J, Chiura T, Marzec KM, Mak PJ. Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy. J Phys Chem B 2021 Apr 15;125(14):3556-3565.
- De Simone G, di Masi A, Ciaccio C, Coletta M, Ascenzi P. NO Scavenging through Reductive Nitrosylation of Ferric Mycobacterium tuberculosis and Homo sapiens Nitrobindins. Int J Mol Sci 2020 Dec 10;21(24).
- Ascenzi P, De Simone G, Sbardella D, Coletta M. Reductive nitrosylation of ferric microperoxidase-11. J Biol Inorg Chem 2019 Feb;24(1):21-29.
- André E, Derrien V, Sebban P, Assrir N, Lescop E, Bernad S. Impact of A90P, F106L and H64V mutations on neuroglobin stability and ligand binding kinetics. J Biol Inorg Chem 2019 Feb;24(1):39-52.
- Ascenzi P, De Simone G, Polticelli F, Gioia M, Coletta M. Reductive nitrosylation of ferric human hemoglobin bound to human haptoglobin 1-1 and 2-2. J Biol Inorg Chem 2018 May;23(3):437-445.
- Ascenzi P, di Masi A, Tundo GR, Pesce A, Visca P, Coletta M. Nitrosylation mechanisms of Mycobacterium tuberculosis and Campylobacter jejuni truncated hemoglobins N, O, and P. PLoS One 2014;9(7):e102811.
- Pesce A, Tilleman L, Donné J, Aste E, Ascenzi P, Ciaccio C, Coletta M, Moens L, Viappiani C, Dewilde S, Bolognesi M, Nardini M. Structure and haem-distal site plasticity in Methanosarcina acetivorans protoglobin. PLoS One 2013;8(6):e66144.
- Tejero J, Basu S, Helms C, Hogg N, King SB, Kim-Shapiro DB, Gladwin MT. Low NO concentration dependence of reductive nitrosylation reaction of hemoglobin. J Biol Chem 2012 May 25;287(22):18262-74.
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