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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
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Electron transfer pathways in a multiheme cytochrome MtrF.

Hiroshi C Watanabe1,2, Yuki Yamashita1, Hiroshi Ishikita3,2

  • 1Department of Applied Chemistry, Graduate School of Engineering, The University of Tokyo, Tokyo 113-8654, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|March 8, 2017
PubMed
Summary

MtrF

Keywords:
Mtr conduitShewanella speciesdecahemedissimilatory metal-reducing bacteriaflavin

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Area of Science:

  • Microbiology and Biochemistry
  • Bioenergetics and Electron Transfer
  • Protein Structure and Function

Background:

  • MtrF is an outer-membrane multiheme cytochrome crucial for extracellular electron transfer.
  • Its 10 heme groups are organized into domains II and IV along a pseudo-C2 axis.
  • Previous simulations suggested symmetrical heme redox potentials and bidirectional electron transfer pathways.

Purpose of the Study:

  • To determine the redox potential (Em) values for all 10 hemes in MtrF.
  • To investigate the influence of protonation states and residue localization on electron transfer pathways.
  • To elucidate the mechanism by which MtrF functions as an electron donor.

Main Methods:

  • Solving the linear Poisson-Boltzmann equation to calculate redox potentials.
  • Incorporating protonation states of titratable residues and heme propionic groups.
  • Analyzing the impact of these factors on electron transfer directionality.

Main Results:

  • Calculated Em values reveal a predominant downhill electron transfer from domain IV to domain II.
  • Acidic residue localization in domain IV drives this directional transfer.
  • Heme reduction alters Em values, enabling alternative downhill pathways to flavin binding sites.

Conclusions:

  • MtrF facilitates directional electron transfer, primarily from domain IV to II, influenced by its amino acid microenvironment.
  • The cytochrome dynamically adjusts electron transfer pathways upon reduction.
  • These findings explain MtrF's role in donating electrons to extracellular targets.