A hemoprotein from azotobacter containing non-heme iron: Isolation and crystallization

Bulen, William A.; LeComte, Jack R.; Lough, Samuel M.

doi:10.1016/0006-291x(73)91125-x

Cited by 40 publications

(20 citation statements)

References 17 publications

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“…The first heme-containing BFR was isolated from A. vinelandii [10], but from closer examination it became clear [11] that this protein had been previously identified in 1973 as a b-type cytochrome [12]. Since then, the presence of bacterioferritins has been established in more than 20 other prokaryotes.…”

Section: Introductionmentioning

confidence: 97%

Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins

Carette

Hagen

Bertrand

et al. 2006

Journal of Inorganic Biochemistry

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Section: Introductionmentioning

confidence: 97%

Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins

Carette

Hagen

Bertrand

et al. 2006

Journal of Inorganic Biochemistry

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“…In 1973, Bulen et al [5] isolated and crystallized a hemoprotein with non-heme iron from Azotobacter, Several years later, this kind of cytochrome protein was identified as a bacterioferritin and speculated as a specific iron-storage depot for nitrogenase and an electronic storage for nitrogen fixation [6]. Whereafter, the bacterioferritin from Azotobacter vinelandii (AvBF) has aroused research interests [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

2.6 Å resolution crystal structure of the bacterioferritin from Azotobacter vinelandii

et al. 2004

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The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a dynamic gating mechanism for shift of the oxidized iron ion. Ba 2þ binding to the fourfold channel implicates that the channel bears Fe 2þ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.

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“…At concentrations as high as 300 pug/ml, no indication of absorption maxima at 417, 530, and 560 nm was observed. Other bacterioferritins exhibit peaks at these wavelengths because of a low protoheme IX content (4,10,24 would be unlike all other bacterioferritins reported to date.…”

mentioning

confidence: 99%

The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin

1993

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The gastric pathogen Helicobacter pylori has been shown to produce a 19.6-kDa protein with apparent binding activity for erythrocytes, human buccal epithelial cells, and laminin. In this report we demonstrate that it is an iron-binding protein, resembling ferritin both structurally and biochemically. Also, because its binding activity for laminin, erythrocytes, and buccal cells was abolished by low concentrations of Tween 20, binding is likely nonspecific.

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A hemoprotein from azotobacter containing non-heme iron: Isolation and crystallization

Cited by 40 publications

References 17 publications

Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins

Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins

2.6 Å resolution crystal structure of the bacterioferritin from Azotobacter vinelandii

The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin

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