Eduardo Perozo

About

Eduardo Perozo, PhD, is the Lillian Eichelberger Cannon Professor of Biochemistry and Molecular Biology at the University of Chicago. He is also a professor of Neuroscience and serves on the Institute Committee on Computational Neuroscience and the Committee on Neurobiology. His research focuses on the structural and functional mechanisms of ion channels, including the pore structure of the Shaker K+ channel, the allosteric activation gating of BK channels, and potassium-dependent structural changes in HERG channels. Additionally, his work explores the folding mechanisms of prestin related to outer hair cell electromotility, the behavior of voltage-sensing domains in proteins like Ci-VSP, and the functional states of ion channels such as CorA and MscS. Dr. Perozo's contributions advance understanding of ion channel gating, conformational states, and membrane protein mechanisms, contributing significantly to the fields of biochemistry, molecular biology, and neuroscience.

Research topics

• Chemistry
• Biology
• Biophysics
• Anatomy
• Computer Science
• Cell biology
• Biochemistry
• Ecology
• Genetics
• Stereochemistry

Selected publications

• The conformational cycle of prestin underlies outer-hair cell electromotility

  Nature · 2021 · 105 citations

  Senior authorCorresponding
  DOI

• Electromechanical coupling in the hyperpolarization-activated K+ channel KAT1

  Nature · 2020 · 80 citations

  Senior authorCorresponding
  DOI

• Mechanism of C-type inactivation in the hERG potassium channel

  Science Advances · 2021 · 48 citations

  channels suggests that C-type inactivation depends on the degree of opening of the intracellular gate via the filter-gate allosteric coupling.

  DOI

• Potassium dependent structural changes in the selectivity filter of HERG potassium channels

  Nature Communications · 2024-08-29 · 22 citations

  articleOpen access

  The fine tuning of biological electrical signaling is mediated by variations in the rates of opening and closing of gates that control ion flux through different ion channels. Human ether-a-go-go related gene (HERG) potassium channels have uniquely rapid inactivation kinetics which are critical to the role they play in regulating cardiac electrical activity. Here, we exploit the K+ sensitivity of HERG inactivation to determine structures of both a conductive and non-conductive selectivity filter…

  PublisherOA PDFDOI

• Structural basis of voltage-dependent gating in BK channels

  Nature Communications · 2025-07-01 · 10 citations

  articleOpen accessSenior author

  Abstract The allosteric communication between the pore domain, voltage sensors, and Ca 2+ binding sites in the calcium- and voltage-activated K + channel (BK) underlies its physiological role as the preeminent signal integrator in excitable systems. BK displays shallow voltage sensitivity with very fast gating charge kinetics, yet little is known about the molecular underpinnings of this distinctive behavior. Here, we explore the mechanistic basis of coupling between voltage-sensing domains (VSD…

  PublisherDOI

Recent grants

• High Resolution Structural Dynamics of K Channels

  NIH · $7.9M · 1998–2020

• NIH Grant R01GM088406

  NIH · $1.3M · 2014

• NIH Grant U54GM087519

  NIH · $63.6M · 2019

Frequent coauthors

• D. Marien Cortés

  Texas Tech University Health Sciences Center

  77 shared

• Luis G. Cuello

  Texas Tech University Health Sciences Center

  54 shared

• Benoı̂t Roux

  University of Chicago

  51 shared

• Valeria Vásquez

  The University of Texas Health Science Center at Houston

  48 shared

• Julio F. Cordero-Morales

  The University of Texas Health Science Center at Houston

  47 shared

• Qufei Li

  University of Chicago

  43 shared

• Francisco Bezanilla

  University of Valparaíso

  37 shared

• Sherry Wanderling

  Howard Hughes Medical Institute

  32 shared

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