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Hemoglobin

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...

Formation of Complex Ions

Formation of Complex Ions

A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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UV–Vis Spectroscopy of Conjugated Systems

UV–Vis Spectroscopy of Conjugated Systems

Organic compounds with conjugated double bonds show strong absorption features in the UV–visible region of the electromagnetic spectrum attributed to π&VeryThinSpace;→&VeryThinSpace;π* electronic excitations. Generally, a UV–vis absorption spectrum is recorded as a plot of absorbance vs wavelength. The wavelength of maximum absorbance, which manifests as a peak in the absorption spectrum, is denoted as λmax.
One of the factors influencing λmax is the extent of conjugation in the...

Gene Families

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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The Equilibrium Binding Constant and Binding Strength

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Updated: Jun 13, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

Published on: August 31, 2018

Hemoglobin-silver interaction and bioconjugate formation: a spectroscopic study.

Mrityunjoy Mahato¹, Prabir Pal, Tapanendu Kamilya

¹Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata-700 032, India.

The Journal of Physical Chemistry. B

|May 4, 2010

Summary

Human hemoglobin (Hb) interacts with silver (Ag), forming a bioconjugate. This interaction alters Hb's structure, indicated by spectroscopic and microscopic analyses, revealing conformational changes and electron transfer.

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

Area of Science:

Bioconjugation science
Protein-silver interactions
Spectroscopic analysis of biomaterials

Background:

Human hemoglobin (Hb) is a vital protein for oxygen transport.
Silver (Ag) nanoparticles are known for their unique properties and applications.
Understanding protein-metal interactions is crucial for developing novel biomaterials.

Purpose of the Study:

To investigate the interaction between human hemoglobin and silver.
To characterize the formation and properties of the resulting Hb-Ag bioconjugate.
To elucidate the conformational changes in Hb upon conjugation with silver.

Main Methods:

UV-vis spectroscopy to study heme group perturbations.
Fluorescence spectroscopy (including time-resolved) to analyze Tryptophan residue environment and quenching mechanisms.
Circular Dichroism (CD) and Fourier-Transform Infrared (FTIR) spectroscopy for secondary structure analysis.
Reduction potential measurements to assess electron transfer.
Field Emission Scanning Electron Microscopy (FE-SEM) and Phase Contrast Inverted Microscopy (PCIM) for visualizing bioconjugate formation.

Main Results:

UV-vis spectra showed perturbation of the soret/heme band, indicating conformational heterogeneity.
Fluorescence studies revealed a more polar environment for Tryptophan residues and identified both static and dynamic quenching mechanisms.
CD and FTIR analyses demonstrated a conversion from alpha-helix to beta-sheet structures, signifying Hb unfolding.
Reduction potential data suggested possible electron transfer between Hb-heme, Ag(+), and Tryptophan.
Microscopy confirmed the formation of the silver-protein bioconjugate.

Conclusions:

Human hemoglobin undergoes significant structural changes upon conjugation with silver.
The interaction involves conformational alterations in both secondary (alpha-helix to beta-sheet) and tertiary structures of Hb.
Spectroscopic and microscopic evidence confirms the formation of a stable Hb-Ag bioconjugate with potential for electron transfer.