Direct Electron Transfer of Human Hemoglobin Molecules on Glass/Tin-Doped Indium Oxide

Martínez-Mancera, Flavio Dolores; Hernández-López, José Luis

doi:10.5772/67806

Cited by 6 publications

(4 citation statements)

References 26 publications

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“…It can be expected that this treatment will change the collagen structure, the water content, the surface roughness and the elasticity of the sample. In the range of 450 nm to 500 nm, we found an apparent increase of the absorption of the scalded skin, which may be caused by the change of the collagen structure, but could also be induced by the oxygenation of Fe 2+ to Fe 3+ in haemoglobin (methaemoglobin), which increases the absorption in the VIS range between 400 nm and 670 nm, especially at the Soret band at around 405 nm [34]. We notice a double peak for the non-scalded skin around 550 nm, which indicates the oxygenation of hemoglobin.…”

Section: Skinmentioning

confidence: 78%

Ex Vivo Determination of Broadband Absorption and Effective Scattering Coefficients of Porcine Tissue

et al. 2021

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A novel approach for precise determination of the optical scattering and absorption properties of porcine tissue using an optimized integrating sphere setup was applied. Measurements on several sample types (skin, muscle, adipose tissue, bone, cartilage, brain) in the spectral range between 400 nm and 1400 nm were performed. Due to the heterogeneity of biological samples, measurements on different individual animals as well as on different sections for each sample type were carried out. For all samples, we used an index matching method to reduce surface roughness effects and to prevent dehydration. The derived absorption spectra were used to estimate the concentration of important tissue chromophores such as water, oxy- and deoxyhemoglobin, collagen and fat.

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Section: Skinmentioning

confidence: 78%

Ex Vivo Determination of Broadband Absorption and Effective Scattering Coefficients of Porcine Tissue

et al. 2021

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“…Distinctively, holo -deoxyHb ZnPPIX embraced a one-power surface-controlled model as i p1,c scales up with υ (curve b) because ZnPPIX now plays as the built-in cofactor of a transmembrane-liked protein, and i p1,c of deoxyHb FePPIX also complied with this rule. Hence, the apparent coverage (Γ) can be reckoned that Γ[deoxyHb ZnPPIX ] = 0.97 and Γ[deoxyHb FePPIX ] = 1.28 pmol/mm 2 , which is thought to be reasonable as Γ[deoxyHb ZnPPIX ]/Γ[deoxyHb FePPIX ] = 75.8% close to the recombination rate ( R = 83%). One step further, by means of the linear slope about E p1,c vs log(υ) and the Laviron equation, the rate constant ( k ) of Fe(III) → Fe(II) could be extrapolated as 4.2 s –1 for oxyHb FePPIX and 3.8 s –1 of Zn(II) → Zn(I) for oxyHb ZnPPIX , which proves to be a competent man-made biocatalyst of comparable electroactivity.…”

Section: Resultsmentioning

confidence: 99%

Electrochemiluminescence-Repurposed Abiological Catalysts in Full Protein Tag for Ultrasensitive Immunoassay

et al. 2020

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Being announced as one of the “2019 Top Ten Emerging Technologies in Chemistry” by IUPAC, the directed evolution of artificial metalloenzymes has led to a broad scope of abiotic processes. Here, inspired by those key proteins in bioluminescence, a rudimentary expression of bio-electrochemiluminescent (ECL) macromolecules was achieved via the complexation of zinc proto-porphyrin IX (ZnPPIX) within apo-hemoglobin (apo-Hb). A high-yield monochromic irradiation at 644 nm could be provoked potentiostatically from the reconstituted holo-HbZnPPIX in solutions. Its secondary structure integrity was elucidated by UV and circular dichroism spectrometry, while voltammetry-hyphenated surface plasmon resonance authenticated its ligation conservativeness in electrical fields. Further conjugation with streptavidin rendered a homogeneous Janus fusion of both receptor and reporter domains, enabling a new abiological catalyst-linked ECL bioassay. On the other hand, singular ZnPPIX inside each tetrameric subunit of Hb accomplished an overall signal amplification without the bother of luminogenic heterojunctions. This pH-tolerant and non-photobleaching optics was essentialized to be the unique configuration interaction between Zn and O2, by which the direct electrochemistry of proteins catalyzed the transient progression of O2 → O2 ·– → O2* + hυ selectively. Such principle was implemented as a signal-on strategy for the determination of a characteristic cancer biomarker, the vascular endothelial growth factor, resulting in competent performance at a low detection limit of 0.6 pg·mL–1 and a wide calibration range along with good stability and reliability in real practices. This simple mutation repurposed the O2-transport Hb in the erythrocytes of almost all vertebrates into a cluster of oxidoreductases with intrinsic ECL activity, which would enrich the chromophore library. More importantly, its genetically engineered variants may come in handy in biomedical diagnosis and visual electrophysiology.

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“…As obtain from soret and Q band peak positions, Hb and GHb contains iron in its ferric state and hence resembles absorption spectrum of methemoglobin. [25] The difference in amplitude of the absorption coefficient is due to the decreased concentrations of heme in glycated hemoglobin. [14] Anemia or iron deficiency is commonly observed in diabetes patients [26,27] and a positive correlation has been observed with heme loss and HbA1c level.…”

Section: Resultsmentioning

confidence: 99%

A Mutagen Acts as a Potent Reducing Agent of Glycated Hemoglobin: a Combined Ultrafast Electron Transfer and Computational Studies

Roy,

Pan,

Ghosh

et al. 2024

ChemBioChem

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Glycated hemoglobin (GHb) found in mammals undergoes irreversible damage when exposed to external redox agents, which is much more vulnerable than its normal counterpart hemoglobin (Hb). Besides the oxygen regulation throughout the body, Hb plays a vital role in balancing immunological health and the redox cycle. Photoinduced ultra‐fast electron transfer phenomena actively participate in regulation of various kind of homeostasis involved in such biomacromolecules. In the present study we have shown that a well‐known mutagen Ethidium Bromide (EtBr) reduces GHb in femtosecond time scale (efficiently) upon photoexcitation after efficient recognition in the biomolecule. We have performed similar experiment by colocalizing EtBr and Iron (Fe(III)) on the micellar surface as Hb mimic in order to study the excited state EtBr dynamics to rationalize the time scale obtained from EtBr in GHb and Hb. While other experimental techniques including Dynamic Light Scattering (DLS), Zeta potential, absorbance and emission spectroscopy have been employed for the confirmation of structural perturbation of GHb compared to Hb, a detailed computational studies involving molecular docking and density functional theory (DFT) have been employed for the explanation of the experimental observations.

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Direct Electron Transfer of Human Hemoglobin Molecules on Glass/Tin-Doped Indium Oxide

Cited by 6 publications

References 26 publications

Ex Vivo Determination of Broadband Absorption and Effective Scattering Coefficients of Porcine Tissue

Ex Vivo Determination of Broadband Absorption and Effective Scattering Coefficients of Porcine Tissue

Electrochemiluminescence-Repurposed Abiological Catalysts in Full Protein Tag for Ultrasensitive Immunoassay

A Mutagen Acts as a Potent Reducing Agent of Glycated Hemoglobin: a Combined Ultrafast Electron Transfer and Computational Studies

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