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Sulfmyoglobin Conformational Change: A Role in the Decrease of Oxy-Myoglobin Functionality.

Elddie Román-Morales1, Erika López-Alfonzo1, Ruth Pietri1

  • 1Department of Chemistry, University of Puerto Rico, Mayagüez Campus, PO BOX 9019, Mayagüez, Puerto Rico 00681-9019.

Biochemistry and Biophysics Reports
|February 1, 2017
PubMed
Summary
This summary is machine-generated.

Hydrogen sulfide (H2S) interaction with myoglobin (Mb) forms sulfmyoglobin (SMb), altering Mb

Keywords:
SAXSWAXShemoglobin I (HbI)hydrogen sulfide (H2S)myoglobin (Mb)sulfmyoglobin (SMb)

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • The physiological role of sulfmyoglobin (SMb), a product of hydrogen sulfide (H2S) interaction with myoglobin (Mb), remains poorly understood.
  • Understanding these interactions is crucial for elucidating Mb's function in various physiological and pathological conditions.

Purpose of the Study:

  • To investigate the structural and conformational changes in myoglobin upon interaction with hydrogen sulfide.
  • To determine the impact of SMb formation on myoglobin's oxygen binding affinity and overall functionality.

Main Methods:

  • Small and Wide Angle X-ray Scattering (SAXS/WAXS) was employed to analyze protein structure.
  • Scattering curves, Guinier, Kratky, Porod, and P(r) plots were analyzed for oxy-myoglobin and oxy-hemoglobin I.
  • Three-dimensional models were generated using SAXS/WAXS data.

Main Results:

  • SMb formation induces significant conformational changes in myoglobin.
  • The protein envelope shows a reduced cleft, indicating increased flexibility and decreased compactness.
  • A direct relationship was observed between structural conformation and protein functionality.

Conclusions:

  • The conformational alterations upon SMb formation contribute to a decreased oxygen affinity in myoglobin.
  • These findings provide insights into the functional consequences of H2S-myoglobin interactions.
  • Further research is warranted to fully elucidate the physiological relevance of SMb.