2011
DOI: 10.1016/j.tim.2011.05.001
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Bioenergetic challenges of microbial iron metabolisms

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Cited by 363 publications
(293 citation statements)
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“…Similar c-type cytochrome-based mechanisms are proposed for microaerophilic Fe(II) oxidation (36). While a number of c-type cytochrome genes are present in the A. ebreus genome, there are no multiheme c-type cytochromes or close homologs of the pio/ fox genes (35). The Dtpsy_1207, Dtpsy_1208, and Dtpsy_2198 gene products have homology with multicopper oxidase family proteins, some of which are known to be involved in Mn(II) oxidation, but these proteins typically utilize oxygen as a cosubstrate to oxidize metals (37) and were never observed in proteomic experiments; therefore, they are unlikely to be involved in NDFO by A. ebreus.…”
Section: Evidence Against An Inducible Fe(ii) Oxidoreductase Inmentioning
confidence: 64%
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“…Similar c-type cytochrome-based mechanisms are proposed for microaerophilic Fe(II) oxidation (36). While a number of c-type cytochrome genes are present in the A. ebreus genome, there are no multiheme c-type cytochromes or close homologs of the pio/ fox genes (35). The Dtpsy_1207, Dtpsy_1208, and Dtpsy_2198 gene products have homology with multicopper oxidase family proteins, some of which are known to be involved in Mn(II) oxidation, but these proteins typically utilize oxygen as a cosubstrate to oxidize metals (37) and were never observed in proteomic experiments; therefore, they are unlikely to be involved in NDFO by A. ebreus.…”
Section: Evidence Against An Inducible Fe(ii) Oxidoreductase Inmentioning
confidence: 64%
“…In the phototrophic iron oxidizers Rhodobacter sp. strain SW2 and Rhodopseudomonas palustris TIE-1, outer membrane porins (PioB), periplasmic multiheme c-type cytochromes (PioA/FoxE), and periplasmic high-potential iron proteins (PioC) or quinoproteins (FoxY) are involved (35). Similar c-type cytochrome-based mechanisms are proposed for microaerophilic Fe(II) oxidation (36).…”
Section: Evidence Against An Inducible Fe(ii) Oxidoreductase Inmentioning
confidence: 81%
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“…In other multiheme cytochromes the heme propionates are often identified as the major contributors to this effect (24). In environments with circumneutral pH, ferrous iron has many different forms with reduction potentials ranging from Ϫ200 mV to almost 400 mV (27). The potentials of the hemes of FoxE are positioned to make the oxidation of many of these iron forms thermodynamically favorable and enable FoxE to perform its predicted task of capturing electrons from Fe(II) to deliver to the photosynthetic reaction center either directly or via a relay of other electron transfer partners (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…A speculative model of the Geobacter EET based on previous research and suggestions [23,31,33,161,162,171,181] is shown in Figure 5.9. This model suggests that electrons are transferred from the menoquinone pool within the inner membrane to MacA which then transfers electrons PpcA [163], which shuttles the electrons across the periplasm to a Pcc complex [33].…”
Section: Abundance Of Eet Related Proteinsmentioning
confidence: 99%