J
John Webb
Researcher at Murdoch University
Publications - 146
Citations - 3446
John Webb is an academic researcher from Murdoch University. The author has contributed to research in topics: Ferritin & Chiton. The author has an hindex of 29, co-authored 145 publications receiving 3244 citations. Previous affiliations of John Webb include University of Washington & Swinburne University of Technology.
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Biomineralization : Chemical and Biochemical Perspectives
TL;DR: The functional forms of biominerals, R.P.Williams crystallochemical strategies in biomineralization, S.Mann and R.C.Perry ferritin - function and structural design of an iron storage protein, P.Webb and C.Birchall.
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A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1.
TL;DR: Several low molecular mass proteins tightly bound to bacterial magnetite were obtained from Magnetospirillum magneticumstrain AMB-1 and showed common features in their amino acid sequences, which may be directly involved in biological magnetite crystal formation in magnetic bacteria.
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Mössbauer spectroscopic studies of the cores of human, limpet and bacterial ferritins
T. G. St. Pierre,Susan Bell,Dominic P. E. Dickson,Stephen Mann,John Webb,Geoffrey R. Moore,R. J. P. Williams +6 more
TL;DR: Ferritin cores from human spleen, limpet (Patella vulgata) haemolymph and bacterial cells have been investigated using 57Fe Mössbauer spectroscopy and show typical superparamagnetic behaviour, while those from the bacterial ferritin show behaviour corresponding to a transition from a magnetically ordered to a paramagnetic state.
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Formation of spherical iron(III) oxyhydroxide nanoparticles sterically stabilized by chitosan in aqueous solutions.
TL;DR: The data support that Chit acts as steric stabilizer and inhibits the macroscopic aggregation of the subcolloidal FeOOH particles, thus the iron(III)-Chit interactions offer a simple and economic way to fabricate nanometric size FeOOh spheres, morphologically similar to the core of iron( III)-storage protein, ferritin.
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Iron chelators of the pyridoxal isonicotinoyl hydrazone class Part II. Formation constants with iron(III) and iron(II)
TL;DR: In this paper, the formation constants for the iron(III) complexes of the orally effective iron chelator pyridoxal isonicotinoyl hydrazone (PIH) and three analogues were determined by a combination of spectrophotometry and potentiometry.