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Related Concept Videos

Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Photosystem I01:27

Photosystem I

Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Photosystems01:32

Photosystems

Photosystems are multiprotein complexes that form the functional units of photosynthesis in plants, algae, and cyanobacteria. They are found embedded in the membrane of tiny sac-like structures called thylakoids placed inside the chloroplast.
Functioning of Photosystems
Photosystems contain many pigment molecules, such as chlorophylls and carotenoids, arranged in a particular organization across two domains — the antenna complex and the reaction center. The main aim of the pigment molecules...
The Photochemical Reaction Center01:29

The Photochemical Reaction Center

Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...

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Related Experiment Video

Updated: May 13, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Primary processes in heme-based sensor proteins.

Ursula Liebl1, Jean-Christophe Lambry, Marten H Vos

  • 1Laboratory for Optics and Biosciences, CNRS, Ecole Polytechnique, Palaiseau, France.

Biochimica Et Biophysica Acta
|March 15, 2013
PubMed
Summary
This summary is machine-generated.

Heme-based sensor proteins act as molecular switches, altering enzymatic activity upon gas ligand binding or dissociation. Their efficient ligand rebinding, or "ligand trap" property, helps stabilize signaling responses.

Keywords:
Heme proteinIntra-protein signalingMolecular dynamicsPrimary processUltrafast spectroscopy

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

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Last Updated: May 13, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
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Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Heme-based sensor proteins are crucial molecular switches.
  • They modulate enzymatic activity via gas ligand (O2, NO, CO) binding to heme.
  • Signal transmission from heme to catalytic sites regulates protein expression.

Purpose of the Study:

  • Review emerging mechanisms in heme-based sensor proteins.
  • Highlight insights from experimental and simulation studies.
  • Focus on intra-protein signaling pathways and ligand dynamics.

Main Methods:

  • Ultrafast optical spectroscopy to study early signaling events.
  • Molecular dynamics simulations for timescale analysis.
  • Review of experimental studies on FixL, CooA, and soluble guanylate cyclase.

Main Results:

  • Heme-ligand bond photolability allows tracking of early signaling.
  • Ligand rebinding to heme is highly efficient in all sensors.
  • Internal ligand mobility in 6-coordinate proteins aids signal transfer.

Conclusions:

  • Heme-based sensors utilize a