@article {3074,
	title = {A Membrane-Bound Cytochrome Enables  To Conserve Energy from Extracellular Electron Transfer.},
	journal = {mBio},
	volume = {10},
	year = {2019},
	month = {2019 Aug 20},
	abstract = {<p>Extracellular electron exchange in  species and closely related  plays an important role in the global carbon cycle and enhances the speed and stability of anaerobic digestion by facilitating efficient syntrophic interactions. Here, we grew  with methanol provided as the electron donor and the humic analogue, anthraquione-2,6-disulfonate (AQDS), provided as the electron acceptor when methane production was inhibited with bromoethanesulfonate. AQDS was reduced with simultaneous methane production in the absence of bromoethanesulfonate. Transcriptomics revealed that expression of the gene for the transmembrane, multiheme, -type cytochrome MmcA was higher in AQDS-respiring cells than in cells performing methylotrophic methanogenesis. A strain in which the gene for MmcA was deleted failed to grow via AQDS reduction but grew with the conversion of methanol or acetate to methane, suggesting that MmcA has a specialized role as a conduit for extracellular electron transfer. Enhanced expression of genes for methanol conversion to methyl-coenzyme M and the Rnf complex suggested that methanol is oxidized to carbon dioxide in AQDS-respiring cells through a pathway that is similar to methyl-coenzyme M oxidation in methanogenic cells. However, during AQDS respiration the Rnf complex and reduced methanophenazine probably transfer electrons to MmcA, which functions as the terminal reductase for AQDS reduction. Extracellular electron transfer may enable the survival of methanogens in dynamic environments in which oxidized humic substances and Fe(III) oxides are intermittently available. The availability of tools for genetic manipulation of  makes it an excellent model microbe for evaluating -type cytochrome-dependent extracellular electron transfer in  The discovery of a methanogen that can conserve energy to support growth solely from the oxidation of organic carbon coupled to the reduction of an extracellular electron acceptor expands the possible environments in which methanogens might thrive. The potential importance of -type cytochromes for extracellular electron transfer to syntrophic bacterial partners and/or Fe(III) minerals in some  was previously proposed, but these studies with  provide the first genetic evidence for cytochrome-based extracellular electron transfer in  The results suggest parallels with Gram-negative bacteria, such as  and  species, in which multiheme outer-surface -type cytochromes are an essential component for electrical communication with the extracellular environment.  offers an unprecedented opportunity to study mechanisms for energy conservation from the anaerobic oxidation of one-carbon organic compounds coupled to extracellular electron transfer in  with implications not only for methanogens but possibly also for  that anaerobically oxidize methane.</p>},
	keywords = {Acetates, Anthraquinones, Cytochromes, Electron Transport, Electrons, Ferric Compounds, Gene Expression Regulation, Archaeal, Gram-Negative Bacteria, Membranes, Mesna, Methane, Methanol, Methanosarcina, Oxidation-Reduction, Oxidoreductases, Transcriptome},
	issn = {2150-7511},
	doi = {10.1128/mBio.00789-19},
	author = {Holmes, Dawn E and Ueki, Toshiyuki and Tang, Hai-Yan and Zhou, Jinjie and Smith, Jessica A and Chaput, Gina and Lovley, Derek R}
}
@article {669,
	title = {Identification of methyl coenzyme M as an intermediate in methanogenesis from acetate in Methanosarcina spp.},
	journal = {J Bacteriol},
	volume = {160},
	year = {1984},
	month = {1984 Nov},
	pages = {521-5},
	abstract = {The transfer of the methyl group of acetate to coenzyme M (2-mercaptoethanesulfonic acid; HS-CoM) during the metabolism of acetate to methane was investigated in cultures of Methanosarcina strain TM-1. The organism metabolized CD3COO- to 83\% CD3H and 17\% CD2H2 and produced no CDH3 or CH4. The isotopic composition of coenzyme M in cells grown on CD3COO- was analyzed with a novel gas chromatography-mass spectrometry technique. The cells contained CD3-D-CoM and CD2H-S-CoM) in a proportion similar to that of CD3H to CD2H2. These results, in conjunction with a report (J.K. Nelson and J.G. Ferry, J. Bacteriol. 160:526-532, 1984) that extracts of acetate-grown strain TM-1 contain high levels of CH3-S-CoM methylreductase, indicate that CH3-S-CoM is an intermediate in the metabolism of acetate to methane in this organism.},
	keywords = {Acetates, Deuterium, Euryarchaeota, Gas Chromatography-Mass Spectrometry, Mercaptoethanol, Mesna, Methane, Methylation},
	issn = {0021-9193},
	author = {Lovley, D R and White, R H and Ferry, J G}
}
@article {670,
	title = {Rapidly growing rumen methanogenic organism that synthesizes coenzyme M and has a high affinity for formate.},
	journal = {Appl Environ Microbiol},
	volume = {48},
	year = {1984},
	month = {1984 Jul},
	pages = {81-7},
	abstract = {Methanogenic bacteria with a coccobacillus morphology similar to Methanobrevibacter ruminantium were isolated from the bovine rumen. One isolate, 10-16B, represented a previously undescribed rumen population that, unlike M. ruminantium, synthesized coenzyme M, grew rapidly (mu = 0.24 h-1) on H2-CO2 in a complex medium, had simple nutritional requirements, and metabolized formate at reported rumen concentrations. H2 was metabolized to partial pressures 10-fold lower than those reported for the rumen. After H2 starvation for 26 h, strain 10-16B rapidly resumed growth when H2 was made available. The minimum concentrations of acetate (6 mM) and ammonia (less than 7 mM) that were required for optimal growth were lower than the reported acetate and ammonia concentrations in the rumen. Isoleucine and leucine stimulated growth, but only at concentrations (greater than 50 microM) higher than those reported for the rumen. Another coccobacillary methanogenic organism that synthesized coenzyme M was isolated from a different animal as were organisms that required an exogenous supply of coenzyme M. In general, methanogenic bacteria that required an exogenous supply of coenzyme M had lower maximum growth rates and more complex nutritional requirements than organisms that synthesized the cofactor. The ability of all isolates to metabolize formate below the detection limit of 10 microM indicated that, in contrast to previous reports, methanogenic bacteria have the potential to directly metabolize formate in the rumen. This study demonstrated that there are physiologically diverse populations of coccobacillary methanogenic bacteria in the rumen that can interact competitively and cooperatively.},
	keywords = {Animals, Cattle, Culture Media, Enzyme Induction, Euryarchaeota, Formates, Hydrogen, Male, Mercaptoethanol, Mesna, Rumen, Substrate Specificity},
	issn = {0099-2240},
	author = {Lovley, D R and Greening, R C and Ferry, J G}
}
