Zobrazeno 1 - 10 of 11 pro vyhledávání: '"J T, Keltjens"'
1
Bacterial Electron Transfer Chains Primed by Proteomics
Autor: H J C T, Wessels, N M, de Almeida, B, Kartal, J T, Keltjens
Publikováno v: Advances in microbial physiology. 68
Electron transport phosphorylation is the central mechanism for most prokaryotic species to harvest energy released in the respiration of their substrates as ATP. Microorganisms have evolved incredible variations on this principle, most of these we p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ac708e603b8bdb543d588dc7ace150f0
https://pubmed.ncbi.nlm.nih.gov/27134025
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3
Adaptation of methane formation and enzyme contents during growth of Methanobacterium thermoautotrophicum (strain deltaH) in a fed-batch fermentor
Autor: J L, Pennings, P, Vermeij, L M, de Poorter, J T, Keltjens, G D, Vogels
Publikováno v: Antonie van Leeuwenhoek. 77(3)
During growth of Methanobacterium thermoautotrophicum in a fed-batch fermentor, the cells are confronted with a steady decrease in the concentration of the hydrogen energy supply. In order to investigate how the organism responds to these changes, ce
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dbd0cd32e836b4363821aa8608751bc6
https://pubmed.ncbi.nlm.nih.gov/15188894
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4
Purification and properties of an enzyme involved in the ATP-dependent activation of the methanol:2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri
Autor: P J, Daas, R W, Wassenaar, P, Willemsen, R J, Theunissen, J T, Keltjens, C, van der Drift, G D, Vogels
Publikováno v: The Journal of biological chemistry. 271(37)
In Methanosarcina barkeri the transfer of the methyl group from methanol to 2-mercaptoethanesulfonic acid is catalyzed by the concerted action of two methyltransferases. The first one is the corrinoid-containing methanol:5-hydroxybenzimidazolylcobami
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1d7b486d9a7fd01788bbdf65f4d5a863
https://pubmed.ncbi.nlm.nih.gov/8798394
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5
Activation mechanism of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri
Autor: P J, Daas, W R, Hagen, J T, Keltjens, C, van der Drift, G D, Vogels
Publikováno v: The Journal of biological chemistry. 271(37)
Methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MT1) is the first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in Methanosarcina barkeri. MT1 only binds the methyl group of methan
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2fda898f10c87f459cd313053a8237f1
https://pubmed.ncbi.nlm.nih.gov/8798395
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6
5-Formyl-5,6,7,8-tetrahydromethanopterin is the intermediate in the process of methanogenesis in Methanosarcina barkeri
Autor: J T, Keltjens, A J, Brugman, J M, Kesseleer, B W, te Brömmelstroet, C, van der Drift, G D, Vogels
Publikováno v: BioFactors (Oxford, England). 3(4)
Formylmethanofuran:tetrahydromethanopterin (H4MPT) formyltransferase and 5,10-methenyl-H4MPT cyclohydrolase purified from Methanosarcina barkeri catalyze a formyl group transfer and the hydrolysis of the methenyl function, respectively. The results f
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::521742febc7fa28e03e721d4ee82a8ba
https://pubmed.ncbi.nlm.nih.gov/1605834
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7
F390 synthetase and F390 hydrolase from Methanobacterium thermoautotrophicum (strain delta H)
Autor: S W, Kengen, H W, von den Hoff, J T, Keltjens, C, van der Drift, G D, Vogels
Publikováno v: BioFactors (Oxford, England). 3(1)
Factor F390 is the 8-OH adenylated form of the deazaflavin coenzyme F420, which is a central electron carrier in methanogenic bacteria. The enzymes catalysing the formation of F390 from ATP and F420 (F390 synthetase) and its hydrolysis into AMP and F
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bbde873aee55474074ec46157dbe0c97
https://pubmed.ncbi.nlm.nih.gov/1647779
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8
Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain delta H
Autor: B W, te Brömmelstroet, C M, Hensgens, J T, Keltjens, C, van der Drift, G D, Vogels
Publikováno v: The Journal of biological chemistry. 265(4)
5,10-Methylenetetrahydromethanopterin reductase was purified 22-fold to apparent homogeneity from the methanogenic bacterium Methanobacterium thermoautotrophicum. The enzyme catalyzes the reduction of 5,10-methylene- to 5-methyltetrahydromethanopteri
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::04c7158c68d031f103b1d64ab32693cd
https://pubmed.ncbi.nlm.nih.gov/2298726
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10
Methanopterin and methanogenic bacteria
Autor: J T, Keltjens, G D, Vogels
Publikováno v: BioFactors (Oxford, England). 1(1)
Methanogenic bacteria comprise a selected group of microorganisms that derive their energy for growth from the hydrogen-dependent reduction of CO2 to methane or the disproportionation of reduced one-carbon compounds and acetate to CO2 and methane. In
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a711a52d52e4100791f7e65892e6a6f2
https://pubmed.ncbi.nlm.nih.gov/3076436
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