Results 51 to 60 of about 9,785 (234)

The genetic basis of energy conservation in the sulfate-reducing bacterium Desulfovibrio alaskensis G20. [PDF]

, 2014
Sulfate-reducing bacteria play major roles in the global carbon and sulfur cycles, but it remains unclear how reducing sulfate yields energy. To determine the genetic basis of energy conservation, we measured the fitness of thousands of pooled mutants of
Arkin, Adam P, Bauer, Stefan, Deutschbauer, Adam M, Kuehl, Jennifer V, Price, Morgan N, Ray, Jayashree, Wetmore, Kelly M   +6 more
core   +1 more source

The Carbon Monoxide Dehydrogenase from Desulfovibrio vulgaris

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2015
Ni-containing Carbon Monoxide Dehydrogenases (CODHs) catalyze the reversible conversion between CO and CO₂and are involved in energy conservation and carbon fixation. These homodimeric enzymes house two NiFeS active sites (C-clusters) and three accessory [4Fe-4S] clusters.
Hadj-Saïd, Jessica, Pandelia, Maria-Eirini, Léger, Christophe, Fourmond, Vincent, Dementin, Sébastien   +4 more
openaire   +3 more sources

Antibiotic-Resistant Desulfovibrio Produces H₂S from Supplements for Animal Farming

Microorganisms, 2023
Sulphate-reducing bacteria, primarily Desulfovibrio, are responsible for the active generation of H2S in swine production waste. The model species for sulphate reduction studies, Desulfovibrio vulgaris strain L2, was previously isolated from swine manure
Olga V. Karnachuk, Alexey V. Beletsky, Andrey L. Rakitin, Olga P. Ikkert, Marat R. Avakyan, Viacheslav S. Zyusman, Andrei Napilov, Andrey V. Mardanov, Nikolai V. Ravin   +8 more
doaj   +1 more source

Selection for novel, acid-tolerant Desulfovibrio spp. from a closed Transbaikal mine site in a temporal pH- gradient bioreactor [PDF]

, 2017
Almost all the known isolates of acidophilic or acid-tolerant sulphate-reducing bacteria (SRB) belong to the spore-forming genus Desulfosporosinus in the Firmicutes.
Antsiferov, Dimtry V., Avakyan, Marat R., Banks, David, Frank, Yulia A., Fyodorova, Tatiana S., Karnachuk, Olga V., Kovalyova, Anastasia A., Lukina, Anastasia, Tuovinen, Olli H.   +8 more
core   +1 more source

A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella [PDF]

, 2012
CymA (tetrahaem cytochrome c) is a member of the NapC/NirT family of quinol dehydrogenases. Essential for the anaerobic respiratory flexibility of shewanellae, CymA transfers electrons from menaquinol to various dedicated systems for the reduction of ...
Butt, Julea N., Bye, Jordan, Cheesman, Myles R., Fredrickson, Jim, Jeuken, Lars J. C., Lowe, Thomas G., Marritt, Sophie J., McMillan, Duncan G. G., Richardson, David J., Shi, Liang, Zachara, John   +10 more
core   +1 more source

Phylogenetic analysis reveals an ancient gene duplication as the origin of the MdtABC efflux pump. [PDF]

, 2020
The efflux pumps from the Resistance-Nodulation-Division family, RND, are main contributors to intrinsic antibiotic resistance in Gram-negative bacteria. Among this family, the MdtABC pump is unusual by having two inner membrane components.
Górecki, Kamil, McEvoy, Megan M
core   +2 more sources

Characterization of a trithionate reductase system from Desulfovibrio vulgaris [PDF]

Journal of Bacteriology, 1985
A trithionate reductase system was isolated and purified from extracts of Desulfovibrio vulgaris. This system reduced trithionate to thiosulfate and consisted of two proteins. One was bisulfite reductase, an enzyme that reduces bisulfite to trithionate, and the second component was designated TR-1.
J H, Kim, J M, Akagi
openaire   +2 more sources

Structural Insights Into CO2 Transport Pathways in a W‐Formate Dehydrogenase: Structural Basis for CO2 Reduction

Angewandte Chemie, Volume 138, Issue 16, 13 April 2026.
Integrated structural analysis of N. vulgaris formate dehydrogenase AB, an enzyme with applications in climate change mitigation, is reported. The substrate/product diffusion pathways were fully mapped, and a retention site was identified that transiently holds substrates and has a key role in CO2‐reducing activity.
Guilherme Vilela‐Alves, Rita Rebelo Manuel, Guilherme Martins, Philippe Carpentier, Agata Raczyńska, Maciej Szaleniec, Inês A. Cardoso Pereira, Maria João Romão, Cristiano Mota   +8 more
wiley   +2 more sources

Homology modeling of the spatial structure of HydSL hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS [PDF]

Компьютерные исследования и моделирование, 2013
The results of homology modeling of HydSL, a NiFe-hydrogenase from purple sulphur bacterium Thiocapsa roseopersicina BBS are presented in this work. It is shown that the models have larger confidence level than earlier published ones; a full-size model ...
Azat Vadimovich Abdullatypov, Anatoly Anatolyevich Tsygankov   +1 more
doaj   +1 more source

Structural Insights into Dissimilatory Sulfite Reductases: Structure of Desulforubidin from Desulfomicrobium Norvegicum [PDF]

, 2011
Dissimilatory sulfite reductases (dSiRs) are crucial enzymes in bacterial sulfur-based energy metabolism, which is likely to have been present in some of the earliest life forms on Earth.
Tania F. Oliveira, Tania F. Oliveira, Edward eFranklin, José P. Afonso, Amir R. Khan, Neil J. Oldham, Inês A. C. ePereira, Margarida eArcher   +7 more
core   +2 more sources