Document Type
Article
Publication Date
2012
Journal or Book Title
Langmuir
Volume
28
Issue
9
First Page
4274
Last Page
4282
DOI
10.1021/la205074n
Abstract
Surface sensitive X-ray scattering and spectroscopic studies have been conducted to determine structural properties of Mms6, the protein in Magnetospirillum magneticum AMB-1 that is implicated as promoter of magnetite nanocrystals growth. Surface pressure versus molecular area isotherms indicate Mms6 forms stable monolayers at the aqueous/vapor interface that are strongly affected by ionic conditions of the subphase. Analysis of X-ray reflectivity from the monolayers shows that the protein conformation at the interface depends on surface pressure and on the presence of ions in the solutions, in particular of iron ions and its complexes. X-ray fluorescence at grazing angles of incidence from the same monolayers allows quantitative determination of surface bound ions to the protein showing that ferric iron binds to Mms6 at higher densities compared to other ions such as Fe 2+ or La 3+ under similar buffer conditions.
Copyright Owner
American Chemical Society
Copyright Date
2012
Language
en
File Format
application/pdf
Recommended Citation
Wang, Wenjie; Bu, Wei; Wang, Lijun; Palo, Pierre E.; Mallapragada, Surya K.; Nilsen-Hamilton, Marit; and Vaknin, David, "Interfacial properties and iron binding to bacterial proteins that promote the growth of magnetite nanocrystals: X-ray reflectivity and surface spectroscopy studies" (2012). Chemical and Biological Engineering Publications. 158.
https://lib.dr.iastate.edu/cbe_pubs/158
Included in
Biochemical and Biomolecular Engineering Commons, Biological and Chemical Physics Commons
Comments
Reprinted (adapted) with permission from Langmuir 28 (2012): pp.4274-4282, doi: 10.1021/la205074n . Copyright 2012 American Chemical Society.