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The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
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In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa
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A natural light-driven inward proton pump.

Keiichi Inoue1,2,3, Shota Ito1, Yoshitaka Kato1

  • 1Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.

Nature Communications
|November 18, 2016
PubMed
Summary
This summary is machine-generated.

Researchers discovered a novel light-driven inward proton (H+) pump in a marine bacterium. This protein, unlike outward pumps, uses weaker electrostatic interactions to transfer protons into cells, revealing intricate molecular control mechanisms.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Light-driven proton (H+) pumps are crucial for energy conversion in nature.
  • Outward H+ pumps are well-characterized, converting light energy into proton motive force.
  • The directionality of proton transfer in these pumps is key to their function.

Purpose of the Study:

  • To characterize a novel, oppositely directed H+ pump.
  • To elucidate the molecular mechanisms controlling proton transfer directionality.
  • To investigate the function of rhodopsins in the marine bacterium Parvularcula oceani.

Main Methods:

  • Expression of bacterial rhodopsins in model systems (E. coli, mouse neural cells).
  • Purification and detailed mechanistic analyses of the identified H+ pump proteins.
  • Comparative analysis of structural and electrostatic interactions at the active center.

Main Results:

  • Identified a light-driven inward H+ pump from Parvularcula oceani.
  • Demonstrated functional inward proton pumping in heterologous expression systems.
  • Revealed that weaker electrostatic interactions at the active center dictate inward proton transfer direction.

Conclusions:

  • The inward H+ pump exhibits a unique molecular design for proton translocation.
  • Subtle differences in active site electrostatics control the direction of proton transfer.
  • This discovery expands our understanding of light-driven energy conversion mechanisms in biological systems.