Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Amyra Treffry"'
Autor:
Charlotte L. Latimer, John R. Guest, Michael A. Quail, Timothy J. Stillman, Pauline M. Harrison, Amyra Treffry, Andrew F. Morland, Peter J. Artymiuk, Simon C. Andrews, Paul P. Connolly
Publikováno v:
Journal of Biological Chemistry. 278:26275-26286
Ferritins are nearly ubiquitous iron storage proteins playing a fundamental role in iron metabolism. They are composed of 24 subunits forming a spherical protein shell encompassing a central iron storage cavity. The iron storage mechanism involves th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f94ec8ebe0e226171e1338d433576c1f
https://doi.org/10.1074/jbc.m207354200
https://doi.org/10.1074/jbc.m207354200
Autor:
Timothy J. Stillman, John R. Guest, Peter J. Artymiuk, Pauline M. Harrison, Amyra Treffry, Simon C. Andrews, P.D. Hempstead, A. J. Hudson
Publikováno v:
Journal of Molecular Biology. 307:587-603
The high-resolution structure of the non-haem ferritin from Escherichia coli (EcFtnA) is presented together with those of its Fe3+ and Zn2+ derivatives, this being the first high-resolution X-ray analysis of the iron centres in any ferritin. The bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a38c7f59e4340581213922d043ea04c7
https://doi.org/10.1006/jmbi.2001.4475
https://doi.org/10.1006/jmbi.2001.4475
Autor:
Zhongwei Zhao, E. R. Bauminger, Michael A. Quail, Pauline M. Harrison, Amyra Treffry, Israel Nowik
Publikováno v:
Inorganica Chimica Acta. 297:171-180
Iron storage in the ferritin of Escherichia coli (EcFtnA) involves (1) the catalytic oxidation of 2Fe(II) at a dinuclear centre (sites A and B) and of a single Fe(II) at a nearby site C; (2) the formation of oxo-bridged Fe(III) dimers (designated ‘
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1722f6bc6335456b618a69e207765d4d
https://doi.org/10.1016/s0020-1693(99)00336-9
https://doi.org/10.1016/s0020-1693(99)00336-9
The use of zinc(II) to probe iron binding and oxidation by the ferritin (EcFtnA) of Escherichia coli
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 3:682-688
The ferritin of Escherichia coli (EcFtnA) is similar to human H-chain ferritin (HuHF) in having 24 subunits, each containing a dinuclear site at which two iron atoms can be oxidised (the diiron centre). In EcFtnA, unlike HuHF, fluorescence quenching
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f4319ad5eb1274ed4e2e802cfd0027a
https://doi.org/10.1007/s007750050282
https://doi.org/10.1007/s007750050282
Publikováno v:
Biochemistry. 36:432-441
The ferroxidase activity of human ferritin has previously been associated with a diiron site situated centrally within the four-helix bundle of H-type chains (HuHF). However, direct information about the site of Fe(II) binding has been lacking, and e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08bb2714fca299535257818bdda2d729
https://doi.org/10.1021/bi961830l
https://doi.org/10.1021/bi961830l
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 1:49-60
Ferritin molecules contain 24 polypeptide chains folded as four-helix bundles and arranged as a hollow shell capable of storing up to 4500 Fe(III) atoms. H chains contain ferroxidase centres which lie within the bundle, about 12 A (1.2 nm) from the o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f6b07720cf466ab4f48710e198d75745
https://doi.org/10.1007/s007750050022
https://doi.org/10.1007/s007750050022
Autor:
John R. Guest, Simon C. Andrews, J. B. Mackey, Pauline M. Harrison, John M. Williams, Chris Hawkins, Amyra Treffry
Publikováno v:
Il Nuovo Cimento D. 18:347-352
This paper describes a preliminary investigation of the mechanisms of Fe(II) oxidation and storage of Fe(III) in the bacterioferritin of Escherichia coli (EcBFR). Using Mossbauer spectroscopy to examine the initial oxidation of iron by EcBFR we have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dca7b1b02ac2ea1cffa32b242d718e78
https://doi.org/10.1007/bf02458916
https://doi.org/10.1007/bf02458916
Publikováno v:
Biochemistry. 34:15204-15213
The iron storage molecule, ferritin, consists of an iron core surrounded by a shell of 24 protein subunits, which, in mammals, are of two types, H and L. Prior to storage of iron as a hydrous ferric oxide within the protein shell, Fe(II) is catalytic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::450c8f226b12eda05db4db9e6297696d
https://doi.org/10.1021/bi00046a028
https://doi.org/10.1021/bi00046a028
Publikováno v:
Journal of Radioanalytical and Nuclear Chemistry Articles. 190:237-241
Iron(III) monomers, dimers and clusters have been identified by Mossbauer spectroscopy during the initial stages of iron incorporation into ferritins, following Fe(II) oxidation. Iron(III) monomers seem to arise from dimer dissociation. Some of the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::639ceb20aca48d266aec9e7129482e12
https://doi.org/10.1007/bf02039998
https://doi.org/10.1007/bf02039998
Publikováno v:
Hyperfine Interactions. 91:835-839
Ferritin stores iron as ferrihydrite inside a shell composed of H and L protein chains. H chains contain ferroxidase centres catalysing Fe2+ oxidation, while L chains lack these centres but seem to promote ferrihydrite nucleation. Mossbauer spectrosc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c403b7f65cd97e4143140b21d10a324a
https://doi.org/10.1007/bf02064615
https://doi.org/10.1007/bf02064615