Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes01:28

Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes

Cytochrome P450 (CYP450) enzymes are a superfamily of heme-containing monooxygenases that play a pivotal role in Phase I drug metabolism by catalyzing oxidation and reduction reactions.These enzymes transform lipophilic xenobiotics into more hydrophilic metabolites, facilitating subsequent Phase II conjugation and eventual excretion. The CYP450 family is classified into families (e.g., CYP1–CYP3) and subfamilies (e.g., CYP2A, CYP2C), based on amino acid sequence homology.CYP450 isoenzymes,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

More about properties of Morse oscillator.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2021
Same author

Nanodiscs in the studies of membrane-bound cytochrome P450 enzymes.

Methods in molecular biology (Clifton, N.J.)·2013
Same author

Cryoradiolysis and cryospectroscopy for studies of heme-oxygen intermediates in cytochromes p450.

Methods in molecular biology (Clifton, N.J.)·2012
Same author

Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscs.

Methods in enzymology·2009
Same author

Protein-membrane interactions: blood clotting on nanoscale bilayers.

Journal of thrombosis and haemostasis : JTH·2009
Same author

Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy.

Biochemistry·2008
Same journal

The chemistry of the cobalt corrinoids - Recent advances and emerging themes. Part 3. Cobalamins and health.

Journal of inorganic biochemistry·2026
Same journal

PIKfyve-specific Pt(II)-based targeted drug conjugate in treatment of ovarian cancer through multi-mode actions.

Journal of inorganic biochemistry·2026
Same journal

From PET to targeted radionuclide therapy in the Brain: The emerging role of radiometal-based platforms.

Journal of inorganic biochemistry·2026
Same journal

The chemistry of the cobalt corrinoids - Recent advances and emerging themes. Part 2. The biochemistry, microbiology, and ecology.

Journal of inorganic biochemistry·2026
Same journal

Substituent effects in picolinic acid-derived silver(I) and zinc(II) complexes: Structure, stability, DNA interactions and therapeutic potential.

Journal of inorganic biochemistry·2026
Same journal

Cadmium(II) imidazole coordination complexes as selective antifungal agents against resistant Candida: Insights into protein binding, electrochemistry, and CYP51 binding predictions.

Journal of inorganic biochemistry·2026
See all related articles

Related Experiment Video

Updated: May 25, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Structural differences between soluble and membrane bound cytochrome P450s.

I G Denisov1, A Y Shih, S G Sligar

  • 1Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA.

Journal of Inorganic Biochemistry
|January 17, 2012
PubMed
Summary
This summary is machine-generated.

Cytochrome P450 enzymes exhibit two distinct structural classes, differing in heme side chain positioning. Membrane-bound P450s show structural shifts facilitating substrate access into lipid bilayers.

More Related Videos

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
08:24

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

Published on: August 18, 2017

Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
12:15

Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy

Published on: February 21, 2019

Related Experiment Videos

Last Updated: May 25, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
08:24

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

Published on: August 18, 2017

Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
12:15

Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy

Published on: February 21, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Cytochrome P450s (CYPs) are a large superfamily of heme monooxygenases found across all kingdoms of life.
  • Despite functional diversity, CYPs share conserved tertiary structures.
  • Understanding structural variations is key to deciphering CYP function, especially concerning substrate access.

Purpose of the Study:

  • To systematically compare X-ray structures of cytochrome P450s to identify distinct structural classes.
  • To investigate the structural implications of membrane binding versus soluble forms of CYPs.
  • To elucidate how structural differences influence substrate access and product escape mechanisms.

Main Methods:

  • Systematic comparison of all available X-ray crystal structures of cytochrome P450 enzymes.
  • Analysis of structural features, including beta-domain and A-propionate heme side chain positioning.
  • Molecular dynamics simulations of human CYP3A4 within a model lipid bilayer (POPC).

Main Results:

  • Two distinct structural classes of cytochrome P450s were identified based on heme side chain positioning.
  • Membrane-bound CYPs (except CYP51) exhibit shifts towards the proximal heme side, potentially enlarging substrate pockets and creating membrane-directed access channels.
  • Molecular dynamics revealed membrane-induced closure of peripheral substrate access channels in CYP3A4, favoring intra-membrane substrate channeling.

Conclusions:

  • A key structural divergence exists between membrane-bound and soluble cytochrome P450s.
  • These structural differences, particularly those involving membrane-interacting helices, have significant functional consequences for substrate processing in lipid environments.
  • The lipid bilayer actively influences CYP structure and substrate access pathways, distinct from buffer conditions.