Results 11 to 20 of about 39,076 (213)

Formate and hydrogen in hydrothermal vents and their use by extremely thermophilic methanogens and heterotrophs

Frontiers in Microbiology, 2023
Extremely thermophilic methanogens in the Methanococci and heterotrophs in the Thermococci are common in deep-sea hydrothermal vents. All Methanococci use H2 as an electron donor, and a few species can also use formate.
James F. Holden, Harita Sistu
doaj   +1 more source

From meadows to milk to mucosa – adaptation of Streptococcus and Lactococcus species to their nutritional environments [PDF]

, 2011
Lactic acid bacteria (LAB) are indigenous to food-related habitats as well as associated with the mucosal surfaces of animals. The LAB family Streptococcaceae consists of the genera Lactococcus and Streptococcus.
Adab, P., Blissett, J., Frew, E., Gill, Paramjit, Griffin, T. L., Griffith, L., Hurley, K. L., Jolly, K., Lancashire, E. R., McGee, E., Pallan, M. J., Parry, J. M., Thompson, J. L.   +12 more
core   +15 more sources

A proteomic view at the biochemistry of syntrophic butyrate oxidation in Syntrophomonas wolfei. [PDF]

PLoS ONE, 2013
In syntrophic conversion of butyrate to methane and CO2, butyrate is oxidized to acetate by secondary fermenting bacteria such as Syntrophomonas wolfei in close cooperation with methanogenic partner organisms, e.g., Methanospirillum hungatei.
Alexander Schmidt, Nicolai Müller, Bernhard Schink, David Schleheck   +3 more
doaj   +1 more source

Anaerobic Carbon Monoxide Dehydrogenase Diversity in the Homoacetogenic Hindgut Microbial Communities of Lower Termites and the Wood Roach [PDF]

, 2011
Anaerobic carbon monoxide dehydrogenase (CODH) is a key enzyme in the Wood-Ljungdahl (acetyl-CoA) pathway for acetogenesis performed by homoacetogenic bacteria.
A Brauman, A Ebert, A Marchler-Bauer, B Soboh, BJ Paster, CL Drennan, CL Drennan, CM Perez, DA Odelson, DM Bodenmiller, E Matson, E Oelgeschläger, E Pezacka, E Pierce, EG Matson, EJ Gagen, Eric G. Matson, F Warnecke, FH Martin, GM King, H Dobbek, HJ Beaumont, HL Drake, HL Drake, HL Drake, HL Drake, J Heo, J Heo, JA Breznak, JA Breznak, Jared R. Leadbetter, JG Ferry, JM González, JR Graber, JR Graber, JR Leadbetter, K Fujinaga, Kasia G. Gora, KH Yeoman, M Köpke, M Pester, M Wu, MA Larkin, MD Kane, R Overbeek, RE Hungate, RL Kerby, S Huang, S Kambhampati, SF Altschul, SW Ragsdale, SW Ragsdale, SW Ragsdale, SW Singer, T Beckwith, TG Lilburn, TI Doukov, TM Salmassi, V Svetlitchnyi, V Svetlitchnyi, Vasu D. Appanna, W Ludwig, X Zhang   +62 more
core   +11 more sources

Structure: Function Studies of the Cytosolic, Mo- and NAD⁺-Dependent Formate Dehydrogenase from Cupriavidus necator

Inorganics, 2020
Here, we report recent progress our laboratories have made in understanding the maturation and reaction mechanism of the cytosolic and NAD+-dependent formate dehydrogenase from Cupriavidus necator. Our recent work has established that the enzyme is fully
Russ Hille, Tynan Young, Dimitri Niks, Sheron Hakopian, Timothy K. Tam, Xuejun Yu, Ashok Mulchandani, Gregor M. Blaha   +7 more
doaj   +1 more source

Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

Communications Biology, 2022
Synthetic carbon monoxide:formate oxidoreductase is designed for direct electron transfer between non-interacting CO dehydrogenase and formate dehydrogenase using an electron-transferring Fe-S fusion protein in T. onnurineus.
Jae Kyu Lim, Ji-In Yang, Yun Jae Kim, Yeong-Jun Park, Yong Hwan Kim   +4 more
doaj   +1 more source

Formate oxidation in the intestinal mucus layer enhances fitness of Salmonella enterica serovar Typhimurium

mBio, 2023
Salmonella enterica serovar Typhimurium induces intestinal inflammation to create a niche that fosters the outgrowth of the pathogen over the gut microbiota.
Maria G. Winter, Elizabeth R. Hughes, Matthew K. Muramatsu, Angel G. Jimenez, Rachael B. Chanin, Luisella Spiga, Caroline C. Gillis, Michael McClelland, Helene Andrews-Polymenis, Sebastian E. Winter   +9 more
doaj   +1 more source

Kinetic studies of formate dehydrogenase [PDF]

Biochemical Journal, 1970
1. The kinetic mechanism of formate dehydrogenase is a sequential pathway. 2. The binding of the substrates proceeds in an obligatory order, NAD+ binding first, followed by formate. 3. It seems most likely that the interconversion of the central ternary complex is extremely rapid, and that the rate-limiting step is the formation or possible ...
D, Peacock, D, Boulter
openaire   +2 more sources

Formate dehydrogenases for CO2 utilization

Current Opinion in Biotechnology, 2022
New measures for reducing atmospheric CO2 are urgently needed. Formate dehydrogenases (FDHs, EC 1.17.1.9) catalyze conversion of CO2 to formate (HCOO-) via a reverse catalytic ability. This enzymatic conversion of CO2 represents a novel first step approach for biocatalytic carbon capture and utilization targeting both CO2 reduction and substitution of ...
Calzadiaz-Ramirez, Liliana, Meyer, Anne S   +1 more
openaire   +3 more sources

Formate dehydrogenase of Clostridium pasteurianum [PDF]

Journal of Bacteriology, 1984
Formate dehydrogenase was purified to electrophoretic homogeneity from N2-fixing cells of Clostridium pasteurianum W5. The purified enzyme has a minimal Mr of 117,000 with two nonidentical subunits with molecular weights of 76,000 and 34,000, respectively.
C L, Liu, L E, Mortenson
openaire   +2 more sources