Identification of an Uptake Hydrogenase Required for Hydrogen-Dependent Reduction of Fe(III) and Other Electron Acceptors by
            <i>Geobacter sulfurreducens</i>

Coppi, Maddalena V.; O'Neil, Regina A.; Lovley, Derek R.

doi:10.1128/jb.186.10.3022-3028.2004

Cited by 89 publications

(86 citation statements)

References 50 publications

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“…Both the wild-type and the SfrAB-null strains were able to grow in Fe(III) citrate medium when either hydrogen or formate was provided as the electron donor (Fig. 2b, c) and a small amount of acetate was provided as a carbon source (1 mM; Coppi et al, 2004). In contrast, only the wild-type strain could grow in Fe(III) citrate medium when acetate was the sole electron donor and carbon source present (Fig.…”

Section: Fe(iii) Reduction By Spheroplastsmentioning

confidence: 91%

“…G. sulfurreducens strain DL1, a wild-type derivative of ATCC 51573 (Caccavo et al, 1994;Coppi et al, 2001), was obtained from our laboratory culture collection. During growth of G. sulfurreducens strains in batch cultures, cells were cultivated anaerobically at 30 uC under an N 2 : CO 2 (80 : 20) atmosphere in two defined liquid freshwater media, NBF and FWFC, which contained 40 mM fumarate or 55 mM Fe(III) citrate, respectively, as the electron acceptor (Lovley & Phillips, 1988;Coppi et al, 2001Coppi et al, , 2004. Acetate (1-15 mM), formate (40 mM), cysteine (1 mM), and antibiotics (200 mg kanamycin ml 21 and/or 400 mg streptomycin ml 21 ) were added from concentrated stock solutions as needed.…”

Section: Methodsmentioning

confidence: 99%

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Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather than intracellular, respiration-linked Fe(III) citrate reduction

et al. 2007

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A soluble ferric reductase, SfrAB, which catalysed the NADPH-dependent reduction of chelated Fe(III), was previously purified from the dissimilatory Fe(III)-reducing micro-organism Geobacter sulfurreducens, suggesting that reduction of chelated forms of Fe(III) might be cytoplasmic. However, metabolically active spheroplast suspensions could not catalyse acetate-dependent Fe(III) citrate reduction, indicating that periplasmic and/or outer-membrane components were required for Fe(III) citrate reduction. Furthermore, phenotypic analysis of an SfrAB knockout mutant suggested that SfrAB was involved in acetate metabolism rather than respiration-linked Fe(III) reduction. The mutant could not grow via the reduction of either Fe(III) citrate or fumarate when acetate was the electron donor but could grow with either acceptor if either hydrogen or formate served as the electron donor. Following prolonged incubation in acetate : fumarate medium in the absence of hydrogen and formate, an 'acetate-adapted' SfrAB-null strain was isolated that was capable of growth on acetate : fumarate medium but not acetate : Fe(III) citrate medium. Comparison of gene expression in this strain with that of the wild-type revealed upregulation of a potential NADPH-dependent ferredoxin oxidoreductase as well as genes involved in energy generation and amino acid uptake, suggesting that NADPH homeostasis and the tricarboxylic acid (TCA) cycle were perturbed in the 'acetate-adapted' SfrAB-null strain. Membrane and soluble fractions prepared from the 'acetate-adapted' strain were depleted of NADPH-dependent Fe(III), viologen and quinone reductase activities. These results indicate that cytoplasmic, respiration-linked reduction of Fe(III) by SfrAB in vivo is unlikely and suggest that deleting SfrAB may interfere with growth via acetate oxidation by interfering with NADP regeneration.

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Section: Fe(iii) Reduction By Spheroplastsmentioning

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather than intracellular, respiration-linked Fe(III) citrate reduction

et al. 2007

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“…Hyb, a periplasmic hydrogenase, was characterized as essential for hydrogen-dependent growth (8,10). The other periplasmic hydrogenase, Hya, is not essential for this process (10). No function was attributed to the two cytoplasmic hydrogenases, Hox and Mvh (8).…”

Section: H Ydrogenases Are Ubiquitous Enzymes Catalyzing the Reversibmentioning

confidence: 99%

“…There are 4 NiFe hydrogenases encoded in the genome of Geobacter sulfurreducens, which has served as a model organism for the study of Geobacteraceae (8,33). Hyb, a periplasmic hydrogenase, was characterized as essential for hydrogen-dependent growth (8,10). The other periplasmic hydrogenase, Hya, is not essential for this process (10).…”

Section: H Ydrogenases Are Ubiquitous Enzymes Catalyzing the Reversibmentioning

confidence: 99%

Role of the NiFe Hydrogenase Hya in Oxidative Stress Defense in Geobacter sulfurreducens

Tremblay

Lovley

2012

J Bacteriol

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Geobacter sulfurreducens , an Fe(III)-reducing deltaproteobacterium found in anoxic subsurface environments, contains 4 NiFe hydrogenases. Hyb, a periplasmically oriented membrane-bound NiFe hydrogenase, is essential for hydrogen-dependent growth. The functions of the three other hydrogenases are unknown. We show here that the other periplasmically oriented membrane-bound NiFe hydrogenase, Hya, is necessary for growth after exposure to oxidative stress when hydrogen or a highly limiting concentration of acetate is the electron source. The beneficial impact of Hya on growth was dependent on the presence of H 2 in the atmosphere. Moreover, the Hya-deficient strain was more sensitive to the presence of superoxide or hydrogen peroxide. Hya was also required to safeguard Hyb hydrogen oxidation activity after exposure to O 2 . Overexpression studies demonstrated that Hya was more resistant to oxidative stress than Hyb. Overexpression of Hya also resulted in the creation of a recombinant strain better fitted for exposure to oxidative stress than wild-type G. sulfurreducens . These results demonstrate that one of the physiological roles of the O 2 -resistant Hya is to participate in the oxidative stress defense of G. sulfurreducens .

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“…G. sulfurreducens strain DL1 (ATCC 51573) and various mutant strains were transferred routinely on NBF medium with 10 mM acetate as the electron donor and 40 mM fumarate as the electron acceptor (Coppi et al, 2004). G. metallireducens strain GS-15 (ATCC 53774) and mutant strains were transferred routinely on FC medium with 10 mM ethanol as electron donor and 55 mM ferric citrate as the electron acceptor (Lovley et al, 1993).…”

Section: Microorganisms Media and Growth Conditionsmentioning

confidence: 99%

Carbon cloth stimulates direct interspecies electron transfer in syntrophic co-cultures

Chen

Rotaru

Liu

et al. 2014

Bioresource Technology

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150

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h i g h l i g h t sConductive carbon cloth stimulated syntrophic metabolism in DIET co-cultures. Carbon cloth did not stimulate metabolism in a co-culture that relied on H 2 transfer. Non-conductive cotton cloth did not facilitate DIET. Carbon cloth restored DIET in Geobacter strains missing pili or OmcS cytochrome. a r t i c l e i n f o t r a c tThis study investigated the possibility that the electrical conductivity of carbon cloth accelerates direct interspecies electron transfer (DIET) in co-cultures. Carbon cloth accelerated metabolism of DIET co-cultures (Geobacter metallireducens-Geobacter sulfurreducens and G. metallireducens-Methanosarcina barkeri) but did not promote metabolism of co-cultures performing interspecies H 2 transfer (Desulfovibrio vulgaris-G. sulfurreducens). On the other hand, DIET co-cultures were not stimulated by poorly conductive cotton cloth. Mutant strains lacking electrically conductive pili, or pili-associated cytochromes participated in DIET only in the presence of carbon cloth. In co-cultures promoted by carbon cloth, cells were primarily associated with the cloth although the syntrophic partners were too far apart for cell-to-cell biological electrical connections to be feasible. Carbon cloth seemingly mediated interspecies electron transfer between the distant syntrophic partners. These results suggest that the ability of carbon cloth to accelerate DIET should be considered in anaerobic digester designs that incorporate carbon cloth.

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Identification of an Uptake Hydrogenase Required for Hydrogen-Dependent Reduction of Fe(III) and Other Electron Acceptors by Geobacter sulfurreducens

Cited by 89 publications

References 50 publications

Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather than intracellular, respiration-linked Fe(III) citrate reduction

Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather than intracellular, respiration-linked Fe(III) citrate reduction

Role of the NiFe Hydrogenase Hya in Oxidative Stress Defense in Geobacter sulfurreducens

Carbon cloth stimulates direct interspecies electron transfer in syntrophic co-cultures

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