Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Nathan B. P. Adams"'
Autor:
Andrew R. J. Murphy, David J. Scanlan, Yin Chen, Nathan B. P. Adams, William A. Cadman, Andrew Bottrill, Gary Bending, John P. Hammond, Andrew Hitchcock, Elizabeth M. H. Wellington, Ian D. E. A. Lidbury
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Here the authors show that 2-aminoethylphosphonate (2AEP) mineralisation is widespread in the global ocean, operating independently of exogenous inorganic phosphate concentration. They propose 2AEP may be a major route for the regeneration of phospha
Externí odkaz:
https://doaj.org/article/ee97040b023c4eed912fd25d3538fa4b
Autor:
Claudine Bisson, Nathan B. P. Adams, Ben Stevenson, Amanda A. Brindley, Despo Polyviou, Thomas S. Bibby, Patrick J. Baker, C. Neil Hunter, Andrew Hitchcock
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
Some bacteria can use inorganic phosphite and hypophosphite as sources of inorganic phosphorus. Here, the authors report crystal structures of the periplasmic proteins that bind these reduced phosphorus species and show that a P-H…π interaction be
Externí odkaz:
https://doaj.org/article/fb628c898a23417e81de94e06a980504
How the O2-dependent Mg-protoporphyrin monomethyl ester cyclase forms the fifth ring of chlorophylls
Publikováno v:
Nature plants
Nature Plants
Nature Plants
Mg-protoporphyrin IX monomethyl ester (MgPME) cyclase catalyses the formation of the isocyclic ring, producing protochlorophyllide a and contributing substantially to the absorption properties of chlorophylls and bacteriochlorophylls. The O2-dependen
Autor:
Nathan B. P. Adams, Andrew Hitchcock, Bethany Johnson, Amanda A. Brindley, Mark J. Dickman, Philip J. Jackson, David A. Farmer, James D. Reid, C. Neil Hunter
Publikováno v:
Biochemical Journal
Magnesium chelatase initiates chlorophyll biosynthesis, catalysing the MgATP2−-dependent insertion of a Mg2+ ion into protoporphyrin IX. The catalytic core of this large enzyme complex consists of three subunits: Bch/ChlI, Bch/ChlD and Bch/ChlH (in
Autor:
Tanja, Bartoschik, Amit, Gupta, Beate, Kern, Andrew, Hitchcock, Nathan B P, Adams, Nuska, Tschammer
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2168
The combination of MicroScale Thermophoresis (MST) and near-native site-specific His-tag labeling enables simple, robust, and reliable determination of the binding affinity between proteins and ligands. To demonstrate its applicability for periplasmi
Autor:
Nathan B P, Adams, Claudine, Bisson, Amanda A, Brindley, David A, Farmer, Paul A, Davison, James D, Reid, C Neil, Hunter
Publikováno v:
Nature plants. 6(12)
The insertion of magnesium into protoporphyrin initiates the biosynthesis of chlorophyll, the pigment that underpins photosynthesis. This reaction, catalysed by the magnesium chelatase complex, couples ATP hydrolysis by a ChlID motor complex to chela
Autor:
Beate Kern, Nathan B. P. Adams, Andrew Hitchcock, Amit J. Gupta, Nuska Tschammer, Tanja Bartoschik
Publikováno v:
Methods in Molecular Biology ISBN: 9781071607237
The combination of MicroScale Thermophoresis (MST) and near-native site-specific His-tag labeling enables simple, robust, and reliable determination of the binding affinity between proteins and ligands. To demonstrate its applicability for periplasmi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1bbe5b67218f3d03c105f325742e7507
https://doi.org/10.1007/978-1-0716-0724-4_2
https://doi.org/10.1007/978-1-0716-0724-4_2
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Phosphorus acquisition is critical for life. In low phosphate conditions, some species of bacteria have evolved mechanisms to import reduced phosphorus compounds, such as phosphite and hypophosphite, as alternative phosphorus sources. Uptake is facil
Publikováno v:
Journal of the American Chemical Society
In chlorophyll biosynthesis, the magnesium chelatase enzyme complex catalyzes the insertion of a Mg(2+) ion into protoporphyrin IX. Prior to this event, two of the three subunits, the AAA(+) proteins ChlI and ChlD, form a ChlID-MgATP complex. We used
Autor:
George A. Sutherland, Andrew Hitchcock, Nathan B. P. Adams, C. Neil Hunter, Fabio Sterpone, Pierre Tufféry, Katie J. Grayson, Dirk B. Auman, Daphne M.J. Mermans, P. Leslie Dutton, Angus J. Robertson, Alexander S. Jones, Colin Robinson, Amanda A. Brindley, Philippe Derreumaux
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6672-6681. ⟨10.1074/jbc.RA117.000880⟩
The Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6672-6681. ⟨10.1074/jbc.RA117.000880⟩
The Journal of Biological Chemistry
Protein transport across the cytoplasmic membrane of bacterial cells is mediated by either the general secretion (Sec) system or the twin-arginine translocase (Tat). The Tat machinery exports folded and cofactor-containing proteins from the cytoplasm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11d47a2941212908a5e7afb119168d42
https://hal.archives-ouvertes.fr/hal-02360042
https://hal.archives-ouvertes.fr/hal-02360042