Interfacial properties and iron binding to bacterial proteins that promote the growth of magnetite nanocrystals: X-ray reflectivity and surface spectroscopy studies.
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.
Ames Laboratory, and Department of Physics and Astronomy, Iowa State University, Ames, Iowa 50011, United States.
Wenjie
W
Wang
Wei
W
Bu
Lijun
L
Wang
Pierre E
PE
Palo
Surya
S
Mallapragada
Marit
M
Nilsen-Hamilton
David
D
Vaknin
D001426:Bacterial Proteins / Q000378:metabolism*; D052203:Ferrosoferric Oxide / Q000737:chemistry*; D007501:Iron / Q000378:metabolism*; D053758:Nanoparticles / Q000737:chemistry*; D036103:Nanotechnology; D011485:Protein Binding
D001426:Bacterial Proteins; D007501:Iron; D052203:Ferrosoferric Oxide