Zobrazeno 1 - 10
of 132
pro vyhledávání: '"Myles A. Cheesman"'
Autor:
Ma Teresa Pellicer Martinez, Jason C Crack, Melissa YY Stewart, Justin M Bradley, Dimitri A Svistunenko, Andrew WB Johnston, Myles R Cheesman, Jonathan D Todd, Nick E Le Brun
Publikováno v:
eLife, Vol 8 (2019)
RirA is a global regulator of iron homeostasis in Rhizobium and related α-proteobacteria. In its [4Fe-4S] cluster-bound form it represses iron uptake by binding to IRO Box sequences upstream of RirA-regulated genes. Under low iron and/or aerobic con
Externí odkaz:
https://doaj.org/article/0b82d755b6fd45c294bb83a3bd369123
Autor:
Leon P. Jenner, Jason C. Crack, Julia M. Kurth, Zuzana Soldánová, Linda Brandt, Katarzyna P. Sokol, Erwin Reisner, Justin M. Bradley, Christiane Dahl, Myles R. Cheesman, Julea N. Butt
Funder: Engineering and Physical Sciences Research Council
Funder: Verband der Chemischen Industrie
Thiosulfate dehydrogenases are bacterial cytochromes that contribute to the oxidation of inorganic sulfur. The active sites of these enzymes
Funder: Verband der Chemischen Industrie
Thiosulfate dehydrogenases are bacterial cytochromes that contribute to the oxidation of inorganic sulfur. The active sites of these enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7059a5fe3a303b72500a479850e76f95
Autor:
Myles R. Cheesman, Sebastian van Helmont, Justin M. Bradley, Julia M. Kurth, Katarzyna P. Sokol, Leon P. Jenner, Christiane Dahl, Julea N. Butt, Erwin Reisner
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry
Journal of Biological Chemistry
Thiosulfate dehydrogenases (TsdA) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions. In contrast to our knowledge of TsdA activities, information on t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd3b896b01091616e0a32e7563ed7786
http://europepmc.org/articles/PMC6879331
http://europepmc.org/articles/PMC6879331
Publikováno v:
Biochemical Journal
Nitrite binding to recombinant wild-type Sperm Whale myoglobin (SWMb) was studied using a combination of spectroscopic methods including room-temperature magnetic circular dichroism. These revealed that the reactive species is free nitrous acid and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::414b1bd2c047a5c14a44f78916e3a8fb
https://ueaeprints.uea.ac.uk/id/eprint/79380/
https://ueaeprints.uea.ac.uk/id/eprint/79380/
Autor:
Andrew J. Gates, Mahmoud A. S. Abdelhamid, Zoë A. E. Waller, Myles R. Cheesman, László Fábián, Colin J. Macdonald
Publikováno v:
Nucleic Acids Research
Previous computational studies have shown that Cu+ can act as a substitute for H+ to support formation of cytosine (C) dimers with similar conformation to the hemi-protonated base pair found in i-motif DNA. Through a range of biophysical methods, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30d105ba4db271b87fc53840987d3d63
https://doi.org/10.1093/nar/gky390
https://doi.org/10.1093/nar/gky390
Autor:
Jason C. Crack, John D. Holmes, Nick E. Le Brun, Ma Teresa Pellicer Martinez, Andrew W. B. Johnston, Myles R. Cheesman, Dimitri A. Svistunenko, Jonathan D. Todd, Ana Bermejo Martínez
Publikováno v:
Chemical Science. 8:8451-8463
Rhizobial iron regulator A (RirA) is a global regulator of iron homeostasis in many nitrogen-fixing Rhizobia and related species of α-proteobacteria. It belongs to the widespread Rrf2 super-family of transcriptional regulators and features three con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::393babdf546119849cdb573d8ad55feb
https://doi.org/10.1039/c7sc02801f
https://doi.org/10.1039/c7sc02801f
Autor:
Melissa Y.Y. Stewart, Ma Teresa Pellicer Martinez, Justin M. Bradley, Jonathan D. Todd, Dimitri A. Svistunenko, Jason C. Crack, Andrew W. B. Johnston, Myles R. Cheesman, Nick E. Le Brun
Publikováno v:
eLife, Vol 8 (2019)
eLife
eLife
RirA is a global regulator of iron homeostasis in Rhizobium and related α-proteobacteria. In its [4Fe-4S] cluster-bound form it represses iron uptake by binding to IRO Box sequences upstream of RirA-regulated genes. Under low iron and/or aerobic con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c20c6ca45804147295e1a1b528607d78
https://elifesciences.org/articles/47804
https://elifesciences.org/articles/47804
Autor:
Ma Teresa Pellicer Martinez, Myles R. Cheesman, Jonathan D. Todd, Melissa Y.Y. Stewart, Jason C. Crack, Justin M. Bradley, Dimitri A. Svistunenko, Nick E. Le Brun, Andrew W. B. Johnston
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::69004dc13ba044638fe7098c4b6c12ca
https://doi.org/10.7554/elife.47804.032
https://doi.org/10.7554/elife.47804.032
Autor:
Vladimir Popov, Thomas G. Lowe, Tamara V. Tikhonova, Julea N. Butt, Sophie J. Marritt, James D. Gwyer, Myles R. Cheesman, Rose-Marie A. S. Doyle
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 18:655-667
The multiheme cytochromes from Thioalkalivibrio nitratireducens (TvNiR) and Escherichia coli (EcNrfA) reduce nitrite to ammonium. Both enzymes contain His/His-ligated hemes to deliver electrons to their active sites, where a Lys-ligated heme has a di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f853473cd4edb9e93e2c1014996dd56
https://doi.org/10.1007/s00775-013-1011-7
https://doi.org/10.1007/s00775-013-1011-7
Autor:
Nicholas J. Watmough, Jessica H. van Wonderen, Vasily S. Oganesyan, Myles R. Cheesman, David J. Richardson, Andrew J. Thomson
Publikováno v:
Biochemical Journal. 451:389-394
Bacterial NOR (nitric oxide reductase) is a major source of the powerful greenhouse gas N 2 O. NorBC from Paracoccus denitrificans is a heterodimeric multi-haem transmembrane complex. The active site, in NorB, comprises high-spin haem b 3 in close pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3217dc4c243c2295208cb2a86a7f408
https://doi.org/10.1042/bj20121406
https://doi.org/10.1042/bj20121406