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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.
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Updated: May 12, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Multi-heme proteins: nature's electronic multi-purpose tool.

Kathryn D Bewley1, Katie E Ellis, Mackenzie A Firer-Sherwood

  • 1Department of Chemistry, Boston University, Boston, MA 02215, USA.

Biochimica Et Biophysica Acta
|April 6, 2013
PubMed
Summary

Multi-heme proteins, containing multiple iron protoporphyrin IX cofactors, are crucial for biological electron transfer and redox reactions. Nature utilizes these complex proteins as modular components in essential biochemical pathways.

Keywords:
Cytochrome cCytochrome c peroxidaseDissimilatory metal reductionElectron transfer

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Last Updated: May 12, 2026

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Published on: December 4, 2017

Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Structural Biology

Background:

  • Iron is a vital nutrient, and its heme cofactor form (iron protoporphyrin IX) is extensively utilized by biological systems.
  • Heme cofactors are increasingly found in multiple copies within single proteins, forming multi-heme proteins.

Purpose of the Study:

  • To review recent advances in the study of multi-heme proteins.
  • To highlight the emergent properties and biological strategies associated with these complex redox proteins.

Main Methods:

  • Literature review of recent research on multi-heme proteins.
  • Analysis of natural strategies and biochemical pathways involving multi-heme proteins.

Main Results:

  • Multi-heme proteins exhibit diverse functions including redox communication and long-range electron transfer.
  • These proteins store reducing/oxidizing equivalents through coupled heme groups.
  • Nature employs multi-heme proteins as modular units in larger biochemical systems.

Conclusions:

  • Multi-heme proteins are essential components in various biological processes, demonstrating sophisticated metal-ion chemistry.
  • Understanding their emergent properties offers insights into bioenergetics and biomimetic systems.