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Review
. 2018 Jul 1:552:50-59.
doi: 10.1016/j.ab.2017.07.009. Epub 2017 Jul 12.

Mitochondrial membrane potential

Ljubava D Zorova  1 , Vasily A Popkov  2 , Egor Y Plotnikov  3 , Denis N Silachev  3 , Irina B Pevzner  3 , Stanislovas S Jankauskas  3 , Valentina A Babenko  2 , Savva D Zorov  4 , Anastasia V Balakireva  5 , Magdalena Juhaszova  6 , Steven J Sollott  6 , Dmitry B Zorov  7
Affiliations
Review

Mitochondrial membrane potential

Ljubava D Zorova et al. Anal Biochem. .

Abstract

The mitochondrial membrane potential (ΔΨm) generated by proton pumps (Complexes I, III and IV) is an essential component in the process of energy storage during oxidative phosphorylation. Together with the proton gradient (ΔpH), ΔΨm forms the transmembrane potential of hydrogen ions which is harnessed to make ATP. The levels of ΔΨm and ATP in the cell are kept relatively stable although there are limited fluctuations of both these factors that can occur reflecting normal physiological activity. However, sustained changes in both factors may be deleterious. A long-lasting drop or rise of ΔΨm vs normal levels may induce unwanted loss of cell viability and be a cause of various pathologies. Among other factors, ΔΨm plays a key role in mitochondrial homeostasis through selective elimination of dysfunctional mitochondria. It is also a driving force for transport of ions (other than H+) and proteins which are necessary for healthy mitochondrial functioning. We propose additional potential mechanisms for which ΔΨm is essential for maintenance of cellular health and viability and provide recommendations how to accurately measure ΔΨm in a cell and discuss potential sources of artifacts.

Keywords: Heterogeneity; Mitochondria; Mitophagy; Quality control; Signaling; Transmembrane potential.

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Conflict of interest statement

The authors claim absence of conflict of interests.

Figures

Fig. 1
Fig. 1
Possible transition of a permeable rhodamine 123 into impermeable rhodamine 110.
Fig. 2
Fig. 2
Transformation of ΔΨ into energy of a rotary motion using a rotor of ATP synthase (left) and bacterial flagellum (right).
See this image and copyright information in PMC

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