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Updated: Jan 23, 2026
05:52
Observation and Analysis of Blinking Surface-enhanced Raman Scattering
Published on: January 11, 2018
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Membrane-mimicking surfaces modulate the heme pocket structure and oxygen affinity in myoglobin: A surface-enhanced
Ulises A Zitare1, Andresa Messias1, Santiago Di Lella2
1Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina; Instituto de Química Física de Los Materiales, Medio Ambiente y Energía (INQUIMAE), Universidad de Buenos Aires-CONICET, Buenos Aires, Argentina.
Colloids and Surfaces. B, Biointerfaces
|January 21, 2026
Summary
Membrane surfaces subtly alter myoglobin (Mb) structure and oxygen binding. This interaction, mimicking mitochondrial membranes, weakens the oxygen bond, facilitating oxygen release and influencing cellular oxygen delivery.
Area of Science:
- Biochemistry
- Biophysics
- Cell Biology
Background:
- Myoglobin (Mb) is crucial for oxygen transport and storage.
- Cellular membranes, particularly the outer mitochondrial membrane, can influence protein function.
- Understanding protein-membrane interactions is key to cellular respiration and oxygen homeostasis.
Purpose of the Study:
- To investigate how membrane-mimicking surfaces affect myoglobin structure and oxygen affinity.
- To explore the role of lysine-rich domains in myoglobin-membrane interactions.
- To elucidate the molecular mechanisms underlying oxygen release influenced by membrane interactions.
Main Methods:
- Utilized surface-enhanced resonance Raman spectroscopy (SERRS) under electrochemical control.
- Employed nanostructured silver electrodes with self-assembled monolayers to model mitochondrial membranes.
- Performed molecular dynamics (MD) simulations to analyze protein-surface interactions.
Main Results:
- Identified lysine-rich domains (helix F and CD region) mediating myoglobin-surface interactions.
- Observed subtle structural changes in myoglobin's heme pocket upon surface interaction.
- Detected spectral evidence of a weakened Fe-O2 bond and decreased oxygen affinity in ferrous OxyMb.
Conclusions:
- Transient interactions with mitochondrial membrane models facilitate myoglobin's oxygen release.
- Structural modulation of the heme pocket by membrane surfaces influences oxygen binding affinity.
- Provides a potential molecular mechanism for how membrane interactions impact cellular oxygen delivery.
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