Recombinant H-chain ferritins: Effects of changes in the 3-fold channels

Amyra Treffry; Pauline M. Harrison; Alessandra Luzzago; Gianni Cesareni

doi:10.1016/0014-5793(89)81350-X

Recombinant H-chain ferritins: Effects of changes in the 3-fold channels

Amyra Treffry, Pauline M. Harrison, Alessandra Luzzago, Gianni Cesareni

Fondazione Santa Lucia

Research output: Contribution to journal › Article › peer-review

Abstract

Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation.

Original language	English
Pages (from-to)	268-272
Number of pages	5
Journal	FEBS Letters
Volume	247
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(89)81350-X
Publication status	Published - Apr 24 1989

Keywords

Ferritin
Ferritin channel
H chain
Iron storage
Iron(III)-apoferritin
Recombinant ferritin

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0014-5793(89)81350-X

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abstract = "Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation.",

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AU - Treffry, Amyra

AU - Harrison, Pauline M.

AU - Luzzago, Alessandra

AU - Cesareni, Gianni

PY - 1989/4/24

Y1 - 1989/4/24

N2 - Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation.

AB - Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation.

KW - Ferritin

KW - Ferritin channel

KW - H chain

KW - Iron storage

KW - Iron(III)-apoferritin

KW - Recombinant ferritin

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Recombinant H-chain ferritins: Effects of changes in the 3-fold channels

Abstract

Keywords

ASJC Scopus subject areas

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