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Hemoglobins: Structural, Functional and Evolutionary Characterization

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (20 February 2025) | Viewed by 6282

Special Issue Editor


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Guest Editor
Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia
Interests: hemoglobins; nitrosative stress; carbonyl stress

Special Issue Information

Dear Colleagues,

Hemoglobins (Hb) are a remarkably widespread group of proteins. They are found in all kingdoms of life and differ in both structure and functions. First discovered in the animal kingdom, they soon were purified from legume nodules, implying that these proteins were more pervasive than previously thought. The term “phytoglobin” is now used for plant hemoglobins. After the discovery of bacterial hemoglobins, the time of their origin was pushed back by several billion years. Hemoglobins’ widespread distribution and ancient origin helped to propose the “Molecular clock” theory.

In recent years, new Hb groups have been described that are very different from the best known erythrocytic Hb, which possesses truncated, pentacoordinated characteristics. Over the past couple of decades, even with well-studied organisms, e.g., those in mammals, “new” hemoglobins have been discovered, such as neuroglobin, cytoglobin, and androglobin. The transport, catalytic, and sensory functions of these proteins have been outlined.

Hb is increasingly important for basic and applied science, implicating several areas of research.

Hemoglobins are explored under various stress conditions including oxidative, nitrosative, and carbonyl stress, and changes in their properties and functioning induced by modifications of the molecule have also been studied. Another aspect of Hb research is biotechnology. This includes Hb expression for practical purposes, as well as the studying of hemoglobins present in small quantities in their environment or the Hb of exotic organisms.

One more widely developed area is “symbiotic” hemoglobins that have specific characteristics related to their functioning in symbiotic systems. Thus, they are also used for biotechnological goals, e.g., Hb of mollusk Lucina pectinata is considered as a hydrogen sulfide scavenger, and the leghemoglobin of legume plants is gaining popularity for its application in so-called “vegetable meat”.

For this Special Issue of International Journal of Molecular Sciences, we are pleased to invite researchers to contribute original research and review articles that showcase recent developments in the structural, functional, and evolutionary characterization of hemoglobins, and demonstrate diverse applications in the process.

Dr. Alexey F. Topunov
Guest Editor

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Keywords

  • hemoglobin
  • phytoglobin
  • leghemoglobin
  • stress conditions
  • biotechnology

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Published Papers (4 papers)

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Research

14 pages, 3267 KiB  
Article
Novel Insights into Hb Shaare Zedek Associated with β0-Thalassemia: Molecular Characteristics, Genetic Origin and Diagnostic Approaches
by Surada Satthakarn, Wibhasiri Srisuwan, Naowarat Kunyanone and Sitthichai Panyasai
Int. J. Mol. Sci. 2024, 25(16), 8578; https://doi.org/10.3390/ijms25168578 - 6 Aug 2024
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Abstract
Hemoglobin Shaare Zedek (Hb SZ) is a rare structural α-Hb variant. Characterizing its genotype–phenotype relationship and genetic origin enhances diagnostic and clinical management insights. We studied a proband and six family members using high-performance liquid chromatography (HPLC), capillary electrophoresis (CE), PCR, and sequencing [...] Read more.
Hemoglobin Shaare Zedek (Hb SZ) is a rare structural α-Hb variant. Characterizing its genotype–phenotype relationship and genetic origin enhances diagnostic and clinical management insights. We studied a proband and six family members using high-performance liquid chromatography (HPLC), capillary electrophoresis (CE), PCR, and sequencing to analyze α- and β-globin genes and α-globin haplotypes. Pathogenicity predictions and a rapid diagnostic method were developed. The proband, his father, grandfather, and aunt had Hb migrating to the HbH-zone on CE and elevated fetal hemoglobin (HbF) on HPLC. Direct sequencing identified an A to G mutation at codon 56 of the α2-globin gene, characteristic of Hb SZ. Additionally, the proband carried a β-globin gene mutation [HBB.52A>T]. Mild thalassemia-like changes were observed in the proband, whereas individuals with only the Hb SZ variant did not exhibit these changes. Pathogenicity predictions indicated that Hb SZ is benign. The variant can be identified using restriction fragment length polymorphism (RFLP) and allele-specific PCR. The Thai variant of Hb SZ is associated with the haplotype [- - M - - - -]. Hb SZ is a non-pathological variant that minimally affects red blood cell parameters, even when it coexists with β0-thalassemia. HPLC and CE systems cannot distinguish it from other Hbs, necessitating DNA analysis for accurate diagnosis. Full article
(This article belongs to the Special Issue Hemoglobins: Structural, Functional and Evolutionary Characterization)
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17 pages, 2560 KiB  
Article
Effects of Nitrosyl Iron Complexes with Thiol, Phosphate, and Thiosulfate Ligands on Hemoglobin
by Olga V. Kosmachevskaya, Elvira I. Nasybullina, Olesya V. Pokidova, Natalia A. Sanina and Alexey F. Topunov
Int. J. Mol. Sci. 2024, 25(13), 7194; https://doi.org/10.3390/ijms25137194 - 29 Jun 2024
Cited by 1 | Viewed by 1250
Abstract
Nitrosyl iron complexes are remarkably multifactorial pharmacological agents. These compounds have been proven to be particularly effective in treating cardiovascular and oncological diseases. We evaluated and compared the antioxidant activity of tetranitrosyl iron complexes (TNICs) with thiosulfate ligands and dinitrosyl iron complexes (DNICs) [...] Read more.
Nitrosyl iron complexes are remarkably multifactorial pharmacological agents. These compounds have been proven to be particularly effective in treating cardiovascular and oncological diseases. We evaluated and compared the antioxidant activity of tetranitrosyl iron complexes (TNICs) with thiosulfate ligands and dinitrosyl iron complexes (DNICs) with glutathione (DNIC-GS) or phosphate (DNIC-PO4) ligands in hemoglobin-containing systems. The studied effects included the production of free radical intermediates during hemoglobin (Hb) oxidation by tert-butyl hydroperoxide, oxidative modification of Hb, and antioxidant properties of nitrosyl iron complexes. Measuring luminol chemiluminescence revealed that the antioxidant effect of TNICs was higher compared to DNIC-PO4. DNIC-GS either did not exhibit antioxidant activity or exerted prooxidant effects at certain concentrations, which might have resulted from thiyl radical formation. TNICs and DNIC-PO4 efficiently protected the Hb heme group from decomposition by organic hydroperoxides. DNIC-GS did not exert any protective effects on the heme group; however, it abolished oxoferrylHb generation. TNICs inhibited the formation of Hb multimeric forms more efficiently than DNICs. Thus, TNICs had more pronounced antioxidant activity than DNICs in Hb-containing systems. Full article
(This article belongs to the Special Issue Hemoglobins: Structural, Functional and Evolutionary Characterization)
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21 pages, 2820 KiB  
Article
The Impact of Virgin and Aged Microstructured Plastics on Proteins: The Case of Hemoglobin Adsorption and Oxygenation
by Florent Saudrais, Marion Schvartz, Jean-Philippe Renault, Jorge Vieira, Stéphanie Devineau, Jocelyne Leroy, Olivier Taché, Yves Boulard and Serge Pin
Int. J. Mol. Sci. 2024, 25(13), 7047; https://doi.org/10.3390/ijms25137047 - 27 Jun 2024
Cited by 2 | Viewed by 1791
Abstract
Plastic particles, particularly micro- and nanoparticles, are emerging pollutants due to the ever-growing amount of plastics produced across a wide variety of sectors. When plastic particles enter a biological medium, they become surrounded by a corona, giving them their biological identity and determining [...] Read more.
Plastic particles, particularly micro- and nanoparticles, are emerging pollutants due to the ever-growing amount of plastics produced across a wide variety of sectors. When plastic particles enter a biological medium, they become surrounded by a corona, giving them their biological identity and determining their interactions in the living environment and their biological effects. Here, we studied the interactions of microstructured plastics with hemoglobin (Hb). Virgin polyethylene microparticles (PEMPs) and polypropylene microparticles (PPMPs) as well as heat- or irradiation-aged microparticles (ag-PEMPs and ag-PPMPs) were used to quantify Hb adsorption. Polypropylene filters (PP-filters) were used to measure the oxygenation of adsorbed Hb. Microstructured plastics were characterized using optical microscopy, SAXS, ATR-FTIR, XPS, and Raman spectroscopy. Adsorption isotherms showed that the Hb corona thickness is larger on PPMPs than on PEMPs and Hb has a higher affinity for PPMPs than for PEMPs. Hb had a lower affinity for ag-PEMPs and ag-PPMPs, but they can be adsorbed in larger amounts. The presence of partial charges on the plastic surface and the oxidation rate of microplastics may explain these differences. Tonometry experiments using an original method, the diffuse reflection of light, showed that adsorbed Hb on PP-filters retains its cooperativity, but its affinity for O2 decreases significantly. Full article
(This article belongs to the Special Issue Hemoglobins: Structural, Functional and Evolutionary Characterization)
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20 pages, 4032 KiB  
Article
Hell’s Gate Globin-I from Methylacidiphilum infernorum Displays a Unique Temperature-Independent pH Sensing Mechanism Utililized a Lipid-Induced Conformational Change
by Brandon J. Reeder, Dimitri A. Svistunenko and Michael T. Wilson
Int. J. Mol. Sci. 2024, 25(12), 6794; https://doi.org/10.3390/ijms25126794 - 20 Jun 2024
Viewed by 1231
Abstract
Hell’s Gate globin-I (HGb-I) is a thermally stable globin from the aerobic methanotroph Methylacidiphilium infernorum. Here we report that HGb-I interacts with lipids stoichiometrically to induce structural changes in the heme pocket, changing the heme iron distal ligation coordination from hexacoordinate to [...] Read more.
Hell’s Gate globin-I (HGb-I) is a thermally stable globin from the aerobic methanotroph Methylacidiphilium infernorum. Here we report that HGb-I interacts with lipids stoichiometrically to induce structural changes in the heme pocket, changing the heme iron distal ligation coordination from hexacoordinate to pentacoordinate. Such changes in heme geometry have only been previously reported for cytochrome c and cytoglobin, linked to apoptosis regulation and enhanced lipid peroxidation activity, respectively. However, unlike cytoglobin and cytochrome c, the heme iron of HGb-I is altered by lipids in ferrous as well as ferric oxidation states. The apparent affinity for lipids in this thermally stable globin is highly pH-dependent but essentially temperature-independent within the range of 20–60 °C. We propose a mechanism to explain these observations, in which lipid binding and stability of the distal endogenous ligand are juxtaposed as a function of temperature. Additionally, we propose that these coupled equilibria may constitute a mechanism through which this acidophilic thermophile senses the pH of its environment. Full article
(This article belongs to the Special Issue Hemoglobins: Structural, Functional and Evolutionary Characterization)
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