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Surface Enhanced Raman Spectroscopy Detection of Biomolecules Using EBL Fabricated Nanostructured Substrates

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Resonance Raman spectroscopy of chemically modified hemoglobins.

F J Bruzzese¹, J A Dix, R P Rava

¹Department of Chemistry, State University of New York, Binghamton 13901.

Biomaterials, Artificial Cells, and Artificial Organs

|January 1, 1990

Summary

Researchers modified human hemoglobin using crosslinking agents to stabilize its structure. Spectroscopic analysis revealed these modifications alter hemoglobin's oxygen transport by influencing the heme iron's spin state.

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Area of Science:

Biochemistry
Biophysics

Background:

Human hemoglobin's oxygen transport is crucial for cellular respiration.
Modifications to hemoglobin structure can alter its oxygen-binding properties.

Purpose of the Study:

To investigate the effects of crosslinking agents on hemoglobin structure and oxygen transport.
To analyze the spin state of heme iron in modified hemoglobin using spectroscopy.

Main Methods:

Hemoglobin was isolated from outdated human blood and stripped of 2,3-diphosphoglycerate.
Crosslinking agents (glyoxalic acid, 1,2-cyclohexadione, fumarate) were used to stabilize the hemoglobin tetramer.
Resonance Raman spectroscopy and absorption spectroscopy were employed to study oxy, deoxy, and fluoro-met hemoglobin forms.

Main Results:

Crosslinking with glyoxalic acid and 1,2-cyclohexadione induced a high-spin state in oxy-hemoglobin.
The same crosslinking agents induced a lower-spin state in fluoro-met hemoglobin.
Spectroscopic data suggest protein constraints at the sixth heme ligand influence the spin state.

Conclusions:

Crosslinking agents significantly alter hemoglobin's structural and electronic properties.
These modifications impact the heme iron's spin state, affecting oxygen transport capability.
Protein-heme interactions play a key role in modulating hemoglobin's functional characteristics.