Zobrazeno 1 - 10
of 34
pro vyhledávání: '"R P, Gunsalus"'
Autor:
K R Sowers, R P Gunsalus
Publikováno v:
Applied and Environmental Microbiology. 61:4382-4388
The methanogenic Archaea, like the Bacteria and Eucarya, possess several osmoregulatory strategies that enable them to adapt to osmotic changes in their environment. The physiological responses of Methanosarcina species to different osmotic pressures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::975099b09a11600fb0fa302a53d85ed6
https://doi.org/10.1128/aem.61.12.4382-4388.1995
https://doi.org/10.1128/aem.61.12.4382-4388.1995
Autor:
Mark T. Werth, Michael K. Johnson, Andrzej T. Kowal, R. P. Gunsalus, Imke Schröder, Annamaria Manodori, Gary Cecchini
Publikováno v:
Biochemistry. 34:12284-12293
Site-directed mutants of Escherichia coli fumarate reductase in which FrdB Cys148, Cys151, Cys154, and Cys158 are replaced individually by Ser have been constructed and overexpressed in a strain of E. coli lacking a wild-type copy of fumarate reducta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ab7aed91138b9b89c9b204136945b0c
https://doi.org/10.1021/bi00038a024
https://doi.org/10.1021/bi00038a024
Publikováno v:
Journal of Bacteriology. 177:4587-4592
Fumarate reductase from Escherichia coli functions both as an anaerobic fumarate reductase and as an aerobic succinate dehydrogenase. A site-directed mutation of E. coli fumarate reductase in which FrdB Pro-159 was replaced with a glutamine or histid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b624ead7ea699f8e246c7fd331552066
https://doi.org/10.1128/jb.177.16.4587-4592.1995
https://doi.org/10.1128/jb.177.16.4587-4592.1995
Publikováno v:
Handbook of Hydrocarbon and Lipid Microbiology ISBN: 9783540775843
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fea863090ed42153b43d5a105ae901b
https://doi.org/10.1007/978-3-540-77587-4_21
https://doi.org/10.1007/978-3-540-77587-4_21
Autor:
Mark T. Werth, Michael K. Johnson, R. P. Gunsalus, Imke Schröder, Anamaria Manodori, Gary Cecchini, Brian A. C. Ackrell
Publikováno v:
Proceedings of the National Academy of Sciences. 87:8965-8969
Site-directed mutants of Escherichia coli fumarate reductase in which each of the four N-terminal cysteine residues in the FrdB subunit, residues 57, 62, 65, and 77, was mutated individually to serine have been constructed, overexpressed, and investi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f769f7c94300dfb4dff55da7a93a6490
https://doi.org/10.1073/pnas.87.22.8965
https://doi.org/10.1073/pnas.87.22.8965
Publikováno v:
Molecular microbiology. 38(5)
The Escherichia coli cydAB operon, encoding the subunits of the high-affinity cytochrome d oxidase, is maximally transcribed in microaerobiosis as a result of the combined action of the oxygen-responsive regulators Fnr and ArcA. Here, we report that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c2fa38d8b1d25ba66ba6011dc3238c63
https://pubmed.ncbi.nlm.nih.gov/11123679
https://pubmed.ncbi.nlm.nih.gov/11123679
Publikováno v:
FEMS microbiology letters. 145(1)
The Escherichia coli modABCD operon, which encodes a high-affinity molybdate uptake system, is transcriptionally regulated in response to molybdate availability by ModE. Here we describe a highly effective enrichment protocol, applicable to any gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e54b4945f92b5dbb21b957572aa9c19b
https://pubmed.ncbi.nlm.nih.gov/8931336
https://pubmed.ncbi.nlm.nih.gov/8931336
Publikováno v:
The Journal of biological chemistry. 268(31)
The mechanisms of gene regulation in the phylogenetic domain Archaea are not yet understood. To examine the expression of a gene encoding a highly regulated catabolic enzyme from the methanogenic archaea, a Methanosarcina thermophila lambda gt11 chro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5bddfde5e1138d9eba2597f66cce7011
https://pubmed.ncbi.nlm.nih.gov/7693685
https://pubmed.ncbi.nlm.nih.gov/7693685
Publikováno v:
The Journal of biological chemistry. 268(2)
Escherichia coli fumarate reductase (FRD) is a four-subunit enzyme that catalyzes the terminal step in anaerobic respiration to fumarate. The hydrophobic FrdC and FrdD subunits anchor the FrdA and FrdB catalytic subunits to the inner surface of the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9149cffa1603c74365dfd5bfe9cf777e
https://pubmed.ncbi.nlm.nih.gov/8419359
https://pubmed.ncbi.nlm.nih.gov/8419359