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Title: Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens

The respiration of metals by the bacterium Geobacter sulfurreducens requires electrons generated by metabolism to pass from the interior of the cell to electron acceptors beyond the cell membranes. The G. sulfurreducens inner membrane multiheme c-type cytochrome ImcH is required for respiration to extracellular electron acceptors with redox potentials greater than - 0.1 V vs. SHE, but ImcH is not essential for electron transfer to lower potential acceptors. In contrast, deletion of cbcL, encoding an inner membrane protein consisting of b-type and multiheme c-type cytochrome domains, severely affected reduction of low potential electron acceptors such as Fe(III)-oxides and electrodes poised at - 0.1 V vs. SHE. Catalytic cyclic voltammetry of a ΔcbcL strain growing on poised electrodes revealed a 50 mV positive shift in driving force required for electron transfer out of the cell. In non-catalytic conditions, low-potential peaks present in wild type biofilms were absent in ΔcbcL mutants. Expression of cbcL in trans increased growth at low redox potential and restored features to cyclic voltammetry. This evidence supports a model where CbcL is a component of a second electron transfer pathway out of the G. sulfurreducens inner membrane that dominates when redox potential is at or below - 0.1more » V vs. SHE.« less
Authors:
 [1] ; ORCiD logo [2] ;  [3]
  1. Univ. of Minnesota, Minneapolis, MN (United States). Dept. of Biochemistry, Molecular Biology, and Biophysics
  2. Univ. of Minnesota, Minneapolis, MN (United States). BioTechnology Inst.
  3. Univ. of Minnesota, Minneapolis, MN (United States). BioTechnology Inst. Dept. of Microbiology
Publication Date:
Grant/Contract Number:
SC0006868; N0001410308
Type:
Published Article
Journal Name:
Bioelectrochemistry (Amsterdam)
Additional Journal Information:
Journal Name: Bioelectrochemistry (Amsterdam); Journal Volume: 107; Journal ID: ISSN 1567-5394
Research Org:
Univ. of Minnesota, Minneapolis, MN (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); Office of Naval Research (ONR) (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; extracellular respiration; metal reduction; Geobacter; cytochrome; microbial electrochemical cell
OSTI Identifier:
1222041
Alternate Identifier(s):
OSTI ID: 1437113

Zacharoff, Lori, Chan, Chi Ho, and Bond, Daniel R. Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens. United States: N. p., Web. doi:10.1016/j.bioelechem.2015.08.003.
Zacharoff, Lori, Chan, Chi Ho, & Bond, Daniel R. Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens. United States. doi:10.1016/j.bioelechem.2015.08.003.
Zacharoff, Lori, Chan, Chi Ho, and Bond, Daniel R. 2015. "Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens". United States. doi:10.1016/j.bioelechem.2015.08.003.
@article{osti_1222041,
title = {Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens},
author = {Zacharoff, Lori and Chan, Chi Ho and Bond, Daniel R.},
abstractNote = {The respiration of metals by the bacterium Geobacter sulfurreducens requires electrons generated by metabolism to pass from the interior of the cell to electron acceptors beyond the cell membranes. The G. sulfurreducens inner membrane multiheme c-type cytochrome ImcH is required for respiration to extracellular electron acceptors with redox potentials greater than - 0.1 V vs. SHE, but ImcH is not essential for electron transfer to lower potential acceptors. In contrast, deletion of cbcL, encoding an inner membrane protein consisting of b-type and multiheme c-type cytochrome domains, severely affected reduction of low potential electron acceptors such as Fe(III)-oxides and electrodes poised at - 0.1 V vs. SHE. Catalytic cyclic voltammetry of a ΔcbcL strain growing on poised electrodes revealed a 50 mV positive shift in driving force required for electron transfer out of the cell. In non-catalytic conditions, low-potential peaks present in wild type biofilms were absent in ΔcbcL mutants. Expression of cbcL in trans increased growth at low redox potential and restored features to cyclic voltammetry. This evidence supports a model where CbcL is a component of a second electron transfer pathway out of the G. sulfurreducens inner membrane that dominates when redox potential is at or below - 0.1 V vs. SHE.},
doi = {10.1016/j.bioelechem.2015.08.003},
journal = {Bioelectrochemistry (Amsterdam)},
number = ,
volume = 107,
place = {United States},
year = {2015},
month = {9}
}