Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization.
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Crystal Structure of Bfr A from Mycobacterium tuberculosis: Incorporation of Selenomethionine Results in Cleavage and Demetallation of HaemMoving Metal Ions through Ferritin−Protein Nanocages from Three-Fold Pores to Catalytic SitesOrganophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenasesNoncovalent self-assembly of a heterotetrameric diiron protein.Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.NMR reveals pathway for ferric mineral precursors to the central cavity of ferritinMoving Fe2+ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates.Iron uptake in ferritin is blocked by binding of [Cr(TREN)(H(2)O)(OH)](2+), a slow dissociating model for [Fe(H(2)O)(6)](2+)The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement.Fe(2+) substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization.Ferritin reactions: direct identification of the site for the diferric peroxide reaction intermediate.Dioxygen activation in soluble methane monooxygenaseOpening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral.Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins.Moving Iron through ferritin protein nanocages depends on residues throughout each four α-helix bundle subunit.Ferritins, iron uptake and storage from the bacterioferritin viewpointMaxi- and mini-ferritins: minerals and protein nanocagesSpectroscopic evidence for and characterization of a trinuclear ferroxidase center in bacterial ferritin from Desulfovibrio vulgaris Hildenborough.Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins.The ferritin Fe2 site at the diiron catalytic center controls the reaction with O2 in the rapid mineralization pathway.Facilitated diffusion of iron(II) and dioxygen substrates into human H-chain ferritin. A fluorescence and absorbance study employing the ferroxidase center substitution Y34W.Protein association and dissociation regulated by ferric ion: a novel pathway for oxidative deposition of iron in pea seed ferritinHuman deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron centerBinding of Pseudomonas aeruginosa apobacterioferritin-associated ferredoxin to bacterioferritin B promotes heme mediation of electron delivery and mobilization of core mineral iron.Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate.Novel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations.Ferritin: the protein nanocage and iron biomineral in health and in disease.Circular dichroism, magnetic circular dichroism, and variable temperature variable field magnetic circular dichroism studies of biferrous and mixed-valent myo-inositol oxygenase: insights into substrate activation of O2 reactivity.Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA).Mechanisms of iron mineralization in ferritins: one size does not fit all.A leucine residue "Gates" solvent but not O2 access to the binding pocket of phascolopsis gouldii hemerythrin.Iron management and production of electricity by microorganisms.Spectroscopic studies of single and double variants of M ferritin: lack of conversion of a biferrous substrate site into a cofactor site for O2 activation.The Ferritin Superfamily.Time-lapse anomalous X-ray diffraction shows how Fe(2+) substrate ions move through ferritin protein nanocages to oxidoreductase sites.The workings of ferritin: a crossroad of opinions.Molecular-Level Insight into the Differential Oxidase and Oxygenase Reactivities of de Novo Due Ferri Proteins.Spectroscopic evidence for the presence of a high-valent Fe(IV) species in the ferroxidase reaction of an archaeal ferritin.Dioxygen activation at non-heme diiron centers: characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase.
P2860
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P2860
Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@en
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@nl
type
label
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@en
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@nl
prefLabel
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@en
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@nl
P2093
P356
P1433
P1476
Direct spectroscopic and kinet ...... fast ferritin mineralization.
@en
P2093
P304
P356
10.1021/BI980847W
P407
P577
1998-07-01T00:00:00Z