Effect of inositol hexakisphosphate on the spectroscopic properties of the nitric oxide derivative of ferrous horse and bovine hemoglobin.
Abstract: The effect of inositol hexakisphosphate (IHP) on the spectroscopic (EPR and absorbance) properties of the nitric oxide derivative of ferrous horse and bovine hemoglobin (Hb) has been investigated. In the absence of IHP, the nitric oxide derivative of ferrous horse Hb shows spectroscopic properties similar to those of the corresponding derivative of ferrous human Hb that are generally taken as typical of the high affinity state of tetrametric hemoproteins. Similar to human Hb, the addition of IHP to the nitric oxide derivative of ferrous horse Hb induces a transition toward a species characterized by spectral properties typical of the low affinity state of hemoglobins. Nevertheless, the equilibrium constant for IHP binding to the nitric oxide derivative of ferrous horse Hb (= 1.5 x 10(2) M-1) is much lower than that reported for the association of the polyphosphate to the same derivative of ferrous human Hb (greater than 3 x 10(5) M-1). Conversely, the spectroscopic properties of the nitric oxide derivative of ferrous bovine Hb are characteristic of the low affinity state of tetrameric hemoproteins, both in the absence and in the presence of IHP. These results, taken together with the behavior of the nitric oxide derivative of ferrous human Hb, provide further evidence for the peculiar oxygen binding properties of horse and bovine Hb.
Publication Date: 1990-10-01 PubMed ID: 1965441DOI: 10.1016/0162-0134(90)80049-4Google Scholar: Lookup
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- Journal Article
Summary
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This research investigated the influence of a biochemical compound, inositol hexakisphosphate (IHP), on the spectroscopic characteristics of the nitric oxide derivative of a specific type of protein found in horse and bovine (cow) blood, known as hemoglobin. The findings indicate that IHP can alter the spectral properties of hemoglobin in horse blood, shifting it towards a state of lower affinity. However, this does not seem to be as effective as when the compound binds with human hemoglobin. The study also noted that hemoglobin in cow’s blood naturally had spectroscopic properties associated with low affinity, with or without the presence of IHP.
About Hemoglobin and Affinity States
- Hemoglobin is a crucial protein in red blood cells that carries oxygen from the lungs to body tissues. This protein has two affinity states: a high oxygen affinity state, where it can effectively bind and carry oxygen, and a low oxygen affinity state, where its ability to bind with oxygen is reduced.
- The switch between these two states is crucial for the efficient transport of oxygen throughout the body.
- The study explored how IHP, a compound found in many organisms including animals, humans, and plants, affects these affinity states in both horse and cow hemoglobin.
Spectroscopic Analysis
- Spectroscopic analysis involves studying how a substance interacts with or produces light, which can provide valuable information about the structure or composition of the substance.
- In this research, the spectroscopic properties of the nitric oxide derivative of ferrous (containing iron) hemoglobin were studied both with and without the addition of IHP.
Findings
- The research found that when IHP is added to the nitric oxide derivative of ferrous horse hemoglobin, it induces a transition to spectral properties typical of low affinity state. This mirrors the behavior seen in human hemoglobin when IHP is added.
- However, the strength of interaction between IHP and the horse hemoglobin (equilibrium constant) is significantly lower than that for human hemoglobin.
- In contrast, the nitric oxide derivative of ferrous bovine hemoglobin already showed spectral properties typical of low affinity states, irrespective of the presence or absence of IHP.
Implications
- This study offers additional evidence that horse and cow hemoglobin possess unique oxygen-binding properties.
- Understanding the specifics of these properties could have implications in fields such as veterinary medicine or research into genetically modified organisms.
Cite This Article
APA
Ascenzi P, Coletta M, Desideri A, Polizio F, Condò SG, Giardina B.
(1990).
Effect of inositol hexakisphosphate on the spectroscopic properties of the nitric oxide derivative of ferrous horse and bovine hemoglobin.
J Inorg Biochem, 40(2), 157-162.
https://doi.org/10.1016/0162-0134(90)80049-4 Publication
Researcher Affiliations
- Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
MeSH Terms
- Animals
- Cattle / blood
- Electron Spin Resonance Spectroscopy
- Hemoglobins / metabolism
- Horses / blood
- Humans
- Nitric Oxide / blood
- Phytic Acid / pharmacology
- Spectrophotometry
Citations
This article has been cited 3 times.- De Simone G, di Masi A, Pesce A, Bolognesi M, Ciaccio C, Tognaccini L, Smulevich G, Abbruzzetti S, Viappiani C, Bruno S, Monaca SD, Pietraforte D, Fattibene P, Coletta M, Ascenzi P. Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties. Int J Mol Sci 2021 Feb 7;22(4).
- Jakubowska MA, Pyka J, Michalczyk-Wetula D, Baczyński K, Cieśla M, Susz A, Ferdek PE, Płonka BK, Fiedor L, Płonka PM. Electron paramagnetic resonance spectroscopy reveals alterations in the redox state of endogenous copper and iron complexes in photodynamic stress-induced ischemic mouse liver. Redox Biol 2020 Jul;34:101566.
- Ascenzi P, Clementi ME, Condò SG, Coletta M, Petruzzelli R, Polizio F, Rizzi M, Giunta C, Peracino V, Giardina B. Functional, spectroscopic and structural properties of haemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra hircus ibex). Biochem J 1993 Dec 1;296 ( Pt 2)(Pt 2):361-5.
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