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Research Project: Impact of Maternal Influence and Early Dietary Factors on Child Growth, Development, and Metabolic Health

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Title: Molecular Insights into Myoglobin Binding Patterns with the Outer Mitochondrial Membrane: A Comparison of Oxygenated and Deoxygenated States

Author
item ANISHKIN, ANDRIY - University Of Maryland
item ADEPU, KIRAN KUMAR - Arkansas Children'S Nutrition Research Center (ACNC)
item BHANDARI, DIPENDRA - Arkansas Children'S Nutrition Research Center (ACNC)
item ADAMS, SEAN - University Of California, Davis
item CHINTAPALLI, SREE - Arkansas Children'S Nutrition Research Center (ACNC)

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 11/12/2023
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Myoglobin (Mb) interaction with the outer mitochondrial membrane (OMM) promotes oxygen (O2) release. However, comprehensive molecular details on specific contact regions of OMM with oxygenated (oxy-) and deoxygenated (deoxy-) Mb are missing. We used molecular dynamics (MD) simulations to explore the interaction of oxy- and deoxy-Mb with the membrane lipids of OMM in two lipid compositions: (a) typical whole membrane on average and (b) specifically the cardiolipin enriched cristae region (contact site). Unrestrained relaxations showed that on an average, both oxy- and deoxy-Mb establish more stable contacts with lipids typical for cristae contact sites rather than average OMM. However, in steered detachment simulations, deoxy-Mb clings tighter to the average OMM and oxy-Mb strongly prefers contact sites of OMM. MD Simulation analysis further indicates that non-specific binding mediated by local electrostatic interactions exists between charged or polar groups of Mb and the membrane for stable interaction. To the best of our knowledge, this is the first computational study providing molecular details of direct Mb-mitochondria interaction that assisted in distinguishing the preferred localization of oxy- and deoxy-Mb on the OMM. Our findings support the existing experimental evidence on Mb-mitochondrial association and shed more insights on Mb-mediated O2 transport for cellular bioenergetics.