Xie, Shenhan, et al. Molecular Catalysis 570 (2025): 114680.
Hemoglobin (Hb), a heme-containing metalloprotein, has been effectively utilized as an oxidase for the green synthesis of quinazoline derivatives via a biocatalytic domino reaction. In this study, bovine hemoglobin (HbBV) was employed as a key catalyst to facilitate oxidative cyclization in an aqueous-organic medium, demonstrating its potential as an eco-friendly alternative to traditional chemical oxidants.
The reaction was conducted in a phosphate-buffered saline (PBS) solution with isopropanol (IPA) as a co-solvent, where HbBV (0.05 mol%) catalyzed the oxidative transformation of quinazoline precursors under mild conditions at room temperature. The reaction progress was monitored using thin-layer chromatography (TLC), and the final products were purified via flash column chromatography. Nuclear magnetic resonance (NMR) spectroscopy confirmed the structural integrity of the synthesized quinazoline derivatives.
Hemoglobin's catalytic efficiency stems from its intrinsic peroxidase-like activity, enabling electron transfer and oxidative processes. The use of hemoglobin in organic synthesis aligns with the principles of green chemistry by minimizing hazardous reagents and promoting biocompatible catalytic systems. This study underscores hemoglobin's versatility as a biocatalyst in the pharmaceutical industry, offering a sustainable and efficient route for the synthesis of bioactive quinazoline scaffolds, which are widely explored for their therapeutic potential in drug discovery.
Nadimifar, Mohammadsadegh, et al. Biomaterials Advances 156 (2024): 213698.
Hemoglobin (Hb)-based oxygen carriers (HBOCs) have emerged as a promising alternative to donor red blood cells (RBCs) for transfusion medicine, addressing challenges such as limited availability, short shelf life, and blood-type compatibility. To enhance the stability and oxygen transport efficiency of HBOCs, a novel metal-phenolic self-assembly approach has been developed for the fabrication of hemoglobin nanoparticles (Hb-NPs).
In this method, Hb-NPs were synthesized using a one-pot assembly in aqueous conditions. Hemoglobin was combined with manganese (Mn²⁺), zinc (Zn²⁺), or zirconium (Zr²⁺) ions, along with tannic acid (TA) and polyethylene glycol (PEG), under controlled stirring conditions. The resulting nanoparticles were purified by centrifugation and stored for further applications. The metal-phenolic coordination not only enhanced the structural stability of Hb but also facilitated the formation of uniform Hb-NPs with improved biocompatibility.
These Hb-NPs offer a promising platform for oxygen delivery in transfusion and emergency medicine, potentially overcoming the limitations of traditional RBC transfusions. The incorporation of metal ions plays a crucial role in tuning the oxygen-binding properties of hemoglobin, making these nanoparticles valuable for therapeutic and biomedical applications. This study highlights the potential of hemoglobin nanotechnology in developing next-generation artificial oxygen carriers with enhanced performance and stability.
Li, Fengxi, et al. Molecular Catalysis 505 (2021): 111519.
Hemoglobin (Hb) has gained significant attention as a biocatalyst in organic synthesis due to its heme-centered redox activity. In this study, hemoglobin from rabbit blood (HbRb) was utilized as a highly efficient catalyst for the synthesis of unsymmetrical trisubstituted 1,3,5-triazines via a green, multicomponent reaction involving isothiocyanates, amidines, and 1,1,3,3-tetramethylguanidine (TMG).
Under optimized conditions (HbRb at 0.05 mol% heme concentration, TBHP as an oxidant, and DMSO as a solvent), this biocatalytic system enabled the rapid synthesis of 1,3,5-triazines at room temperature within 10 minutes, yielding up to 96%. Comparative studies with other hemoproteins and ferric-based chemical catalysts demonstrated that HbRb exhibited superior catalytic performance, emphasizing the critical role of its active conformation and heme center.
Control experiments using Apo-HbRb or denatured HbRb resulted in significantly lower yields, indicating that the structural integrity of hemoglobin is essential for catalytic activity. The reaction proceeded via a non-Fenton radical pathway, further distinguishing hemoglobin's role as a selective oxidative biocatalyst.
This study highlights the potential of HbRb as an eco-friendly, cost-effective catalyst for complex organic transformations, offering a sustainable alternative to traditional metal-based catalysts in green chemistry.
What is the product name of the substance with CAS number 9008-02-0?
The product name is Hemoglobin.
What is the IUPAC name of Hemoglobin?
The IUPAC name is 2-(furan-2-yl)-7-methyl-1H-1,8-naphthyridin-4-one.
What is the molecular weight of Hemoglobin?
The molecular weight is 226.23.
What is the molecular formula of Hemoglobin?
The molecular formula is C13H10N2O2.
What is the SMILES notation for Hemoglobin?
The SMILES notation is CC1=NC2=C(C=C1)C(=O)C=C(N2)C3=CC=CO3.
What is the InChI for Hemoglobin?
The InChI is INGWEZCOABYORO-UHFFFAOYSA-N.
What is the InChI Key for Hemoglobin?
The InChI Key is InChI=1S/C13H10N2O2/c1-8-4-5-9-11(16)7-10(15-13(9)14-8)12-3-2-6-17-12/h2-7H,1H3,(H,14,15,16).
What is the percentage of actives in Hemoglobin?
The percentage of actives in Hemoglobin is 90%.
What is the physical state of Hemoglobin?
The physical state is solid.
What is the chemical structure of Hemoglobin composed of?
The chemical structure is a fused ring system consisting of a furan ring and a naphthyridine ring with a carbonyl group.
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