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Title: Rational engineering of Geobacter sulfurreducens electron transfer components: A foundation for building improved Geobacter-based bioelectrochemical technologies

Journal Article · · Frontiers in Microbiology
 [1];  [1];  [2];  [3];  [4];  [4];  [4];  [1]
  1. Univ. Nova de Lisboa, Caparica (Portugal)
  2. Towson Univ., Towson, MD (United States)
  3. Instituto de Quimica-Fisica "Rocasolano", Madrid (Spain)
  4. Argonne National Lab. (ANL), Lemont, IL (United States)

Multiheme cytochromes have been implicated in Geobacter sulfurreducens extracellular electron transfer (EET). These proteins are potential targets to improve EET and enhance bioremediation and electrical current production by G. sulfurreducens. However, the functional characterization of multiheme cytochromes is particularly complex due to the co-existence of several microstates in solution, connecting the fully reduced and fully oxidized states. Throughout the last decade, new strategies have been developed to characterize multiheme redox proteins functionally and structurally. These strategies were used to reveal the functional mechanism of G. sulfurreducens multiheme cytochromes and also to identify key residues in these proteins for EET. In previous studies, we set the foundations for enhancement of the EET abilities of G. sulfurreducens by characterizing a family of five triheme cytochromes (PpcA-E). These periplasmic cytochromes are implicated in electron transfer between the oxidative reactions of metabolism in the cytoplasm and the reduction of extracellular terminal electron acceptors at the cell's outer surface. The results obtained suggested that PpcA can couple e-/H+ transfer, a property that might contribute to the proton electrochemical gradient across the cytoplasmic membrane for metabolic energy production. The structural and functional properties of PpcA were characterized in detail and used for rational design of a family of 23 single site PpcA mutants. In this review, we summarize the functional characterization of the native and mutant proteins. Mutants that retain the mechanistic features of PpcA and adopt preferential e-/H+ transfer pathways at lower reduction potential values compared to the wild-type protein were selected for in vivo studies as the best candidates to increase the electron transfer rate of G. sulfurreducens. For the first time G. sulfurreducens strains have been manipulated by the introduction of mutant forms of essential proteins with the aim to develop and improve bioelectrochemical technologies.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1224905
Journal Information:
Frontiers in Microbiology, Vol. 6; ISSN 1664-302X
Publisher:
Frontiers Research FoundationCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 28 works
Citation information provided by
Web of Science

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Cited By (5)

Potential regulates metabolism and extracellular respiration of electroactive Geobacter biofilm journal February 2019
Silica immobilization of Geobacter sulfurreducens for constructing ready-to-use artificial bioelectrodes journal April 2017
Chasing bacterial chassis for metabolic engineering: a perspective review from classical to non-traditional microorganisms journal June 2018
Potential of Zymomonas mobilis as an electricity producer in ethanol production journal March 2020
The triheme cytochrome PpcF from Geobacter metallireducens exhibits distinct redox properties journal November 2018

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