Results 41 to 50 of about 23,949 (213)

Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus hydrogenoformans [PDF]

Journal of Bacteriology, 2001
ABSTRACT Two monofunctional NiFeS carbon monoxide (CO) dehydrogenases, designated CODH I and CODH II, were purified to homogeneity from the anaerobic CO-utilizing eubacterium Carboxydothermus hydrogenoformans .
V, Svetlitchnyi, C, Peschel, G, Acker, O, Meyer   +3 more
openaire   +2 more sources

Current status of carbon monoxide dehydrogenases (CODH) and their potential for electrochemical applications

Bioresources and Bioprocessing, 2023
Anthropogenic carbon dioxide (CO2) levels are rising to alarming concentrations in earth’s atmosphere, causing adverse effects and global climate changes.
Rebecca Bährle, Stefanie Böhnke, Jonas Englhard, Julien Bachmann, Mirjam Perner   +4 more
doaj   +1 more source

Studies of carbon monoxide dehydrogenase from Oligotropha carboxidovorans [PDF]

Journal of Molecular Catalysis B: Enzymatic, 2016
Abstract We have undertaken physicochemical studies of the CO dehydrogenase from the aerobe Oligotropha carboxidovorans, probing both the binuclear Mo- and Cu-containing active site where CO is oxidized to CO2 and the enzyme’s FAD, where the reducing equivalents obtained from CO are transferred to the quinone pool.
Stephanie Dingwall, Jarett Wilcoxen, Dimitri Niks, Russ Hille   +3 more
openaire   +1 more source

Functional and Biogenetical Heterogeneity of the Inner Membrane of Rat-Liver Mitochondria [PDF]

, 1971
Rat liver mitochondria were fragmented by a combined technique of swelling, shrinking, and sonication. Fragments of inner membrane were separated by density gradient centrifugation.
Allmann D. W., Ashwell M., Beattie D. S., Beattie D. S., Brunner G., Burstone M. S., Davis K. A., Delbruck A., Fiske C. H., Folch J., Gear A. R. L., Gear A. R. L., Gear A. R. L., Gelder B. F., Gotterer G. S., Hasegawa E., Hawley E. S., Johnson A. B., Klingenberg M., Kuntzel H., Labbe R. F., Lentz P. E., Neupert W., Neupert W., Novikoff A. B., Ohnishi K., Omura T., Parsons D. F., Parsons D. F., Pette D., Pollak J. K., Pullmann M. E., Raw J., Raw J., Reith A., Schneider W. C., Schuel H., Schumacher H.-H., Sebald W., Sebald W., Seligman A. M., Sies H., Sottocasa G. L., Stoffel W., Strecker H. J., Swick R. W., Szarkowska L., Tabor C. W., Tol A., Vazquez J. J., Yonetani T.   +50 more
core   +1 more source

Carbon monoxide dehydrogenase and acetate thiokinase inMethanothrix soehngenii [PDF]

FEMS Microbiology Letters, 1984
In Methanothrix soehngenii acetate is first activated by an acetate thiokinase rather than a phosphotransacetylase. The specific activity of the acetate thiokinase was 5.29 μmol acetate activated min−1 mg−1 protein with a half maximum rate at 0.74 mM acetate and at 0.047 mM CoA.
Kohler, H.P.E., Zehnder, A.J.B.
openaire   +2 more sources

Insights into the Ecological Roles and Evolution of Methyl-Coenzyme M Reductase-Containing Hot Spring Archaea [PDF]

, 2019
Several recent studies have shown the presence of genes for the key enzyme associated with archaeal methane/alkane metabolism, methyl-coenzyme M reductase (Mcr), in metagenome-assembled genomes (MAGs) divergent to existing archaeal lineages.
Chen, Ya-Ting, Evans, Paul N., Goh, Kian Mau, Hedlund, Brian P., Hozzein, Wael, Hua, Zheng-Shuang, Huang, Min-Jun, Jiao, Jian-Yu, Li, Wen-Jun, Li, Yu-Xian, Mao, Yan-Ping, Qi, Yan-Ling, Qu, Yan-Ni, Rao, Yang-Zhi, Shu, Wen-Sheng, Tyson, Gene W., Wang, Yu-Lin, Zhang, Tong   +17 more
core   +3 more sources

Investigations of the Efficient Electrocatalytic Interconversions of Carbon Dioxide and Carbon Monoxide by Nickel-Containing Carbon Monoxide Dehydrogenases [PDF]

, 2014
Carbon monoxide dehydrogenases (CODH) play an important role in utilizing carbon monoxide (CO) or carbon dioxide (CO2) in the metabolism of some microorganisms. Two distinctly different types of CODH are distinguished by the elements constituting the active site.
Vincent C-C, Wang, Stephen W, Ragsdale, Fraser A, Armstrong   +2 more
openaire   +2 more sources

Carbon monoxide fermentation to ethanol by Clostridium autoethanogenum in a bioreactor with no accumulation of acetic acid [PDF]

, 2015
[Abstract] Fermentation of CO or syngas offers an attractive route to produce bioethanol. However, during the bioconversion, one of the challenges to overcome is to reduce the production of acetic acid in order to minimize recovery costs.
Kennes, Christian, Nalakath Abubackar, Haris, Veiga, María Carmen   +2 more
core   +2 more sources

Purification and properties of carbon monoxide dehydrogenase from Methanococcus vannielii [PDF]

Journal of Bacteriology, 1987
Carbon monoxide dehydrogenase was purified to homogeneity from Methanococcus vannielii grown with formate as the sole carbon source. The enzyme is composed of subunits with molecular weights of 89,000 and 21,000 in an alpha 2 beta 2 oligomeric structure. The native molecular weight of carbon monoxide dehydrogenase, determined by gel electrophoresis, is
E, DeMoll, D A, Grahame, J M, Harnly, L, Tsai, T C, Stadtman   +4 more
openaire   +2 more sources

Bioinspired iron porphyrins with appended poly-pyridine/amine units for boosted electrocatalytic CO2 reduction reaction

eScience, 2022
Developing highly efficient electrocatalysts for the CO2 reduction reaction (CO2RR) has attracted increasing interest in the past decade. Herein, we report on the design and synthesis of Fe porphyrin 1 with an appended N,N-di(2-picolyl)ethylenediamine ...
Jinxiu Han, Ni Wang, Xialiang Li, Haitao Lei, Yabo Wang, Hongbo Guo, Xiaotong Jin, Qingxin Zhang, Xinyang Peng, Xue-Peng Zhang, Wei Zhang, Ulf-Peter Apfel, Rui Cao   +12 more
doaj   +1 more source