Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein

Poppe J, Warkentin E, Demmer U, Kowalewski B, Dierks T, Schneider K, Ermler U (2014)
Journal of Inorganic Biochemistry 138: 122-128.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The molybdenum storage protein (MoSto) can store more than 100 Mo or W atoms as discrete polyoxometalate (POM) clusters. Here, we describe the three POM cluster sites along the threefold axis of the protein complex based on four X-ray structures with slightly different polyoxomolybdate compositions between 1.35 and 2 angstrom resolution. In contrast to the Mo alpha-out binding site occupied by an Mo-3 cluster, the Mo alpha-in and Mo-beta binding sites contain rather weak and non-uniform electron density for the Mo atoms (but clearly identifiable by anomalous data), suggesting the presence of POM cluster ensembles and/or degradation products of larger aggregates. The "Mo alpha-in cluster ensemble" was interpreted as an antiprism-like Mo-6 species superimposed with an Mo-7 pyramide and the "Mo-beta cluster ensemble" as an Mo-13 cluster (present mostly ins degraded form) composed of a pyramidal Mo-7 and a Mo-3 building block linked by three spatially separated MoOx units. Inside the ball-shaped Mo-13 cluster sits an occluded central atom, perhaps a metal ion. POM cluster formation at the Mo alpha-in, and Mo-beta sites appears to be driven by filtering out and binding/protecting self-assembled transient species complementary to the protein template. (C) 2014 Elsevier Inc. All rights reserved.
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Journal of Inorganic Biochemistry
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138
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122-128
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Poppe J, Warkentin E, Demmer U, et al. Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. Journal of Inorganic Biochemistry. 2014;138:122-128.
Poppe, J., Warkentin, E., Demmer, U., Kowalewski, B., Dierks, T., Schneider, K., & Ermler, U. (2014). Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. Journal of Inorganic Biochemistry, 138, 122-128. doi:10.1016/j.jinorgbio.2014.05.009
Poppe, J., Warkentin, E., Demmer, U., Kowalewski, B., Dierks, T., Schneider, K., and Ermler, U. (2014). Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. Journal of Inorganic Biochemistry 138, 122-128.
Poppe, J., et al., 2014. Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. Journal of Inorganic Biochemistry, 138, p 122-128.
J. Poppe, et al., “Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein”, Journal of Inorganic Biochemistry, vol. 138, 2014, pp. 122-128.
Poppe, J., Warkentin, E., Demmer, U., Kowalewski, B., Dierks, T., Schneider, K., Ermler, U.: Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein. Journal of Inorganic Biochemistry. 138, 122-128 (2014).
Poppe, Juliane, Warkentin, Eberhard, Demmer, Ulrike, Kowalewski, Björn, Dierks, Thomas, Schneider, Klaus, and Ermler, Ulrich. “Structural diversity of polyoxomolybdate clusters along the three-fold axis of the molybdenum storage protein”. Journal of Inorganic Biochemistry 138 (2014): 122-128.

4 Zitationen in Europe PMC

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Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion.
Sippel D, Schlesier J, Rohde M, Trncik C, Decamps L, Djurdjevic I, Spatzal T, Andrade SL, Einsle O., J Biol Inorg Chem 22(1), 2017
PMID: 27928630
A survey of the different roles of polyoxometalates in their interaction with amino acids, peptides and proteins.
Arefian M, Mirzaei M, Eshtiagh-Hosseini H, Frontera A., Dalton Trans 46(21), 2017
PMID: 28530742

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