Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters

Kowalewski B, Poppe J, Demmer U, Warkentin E, Dierks T, Ermler U, Schneider K (2012)
Journal of the American Chemical Society 134(23): 9768-9774.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
Some N-2-fixing bacteria prolong the functionality of nitrogenase in molybdenum starvation by a special Mo storage protein (MoSto) that can store more than 100 Mo atoms. The presented 1.6 angstrom X-ray structure of MoSto from Azotobacter vinelandii reveals various discrete polyoxomolybdate clusters, three covalently and three noncovalently bound Mo-8, three Mo5-7, and one Mo-3 clusters, and several low occupied, so far undefinable clusters, which are embedded in specific pockets inside a locked cage-shaped (alpha beta)(3) protein complex. The structurally identical Mo-8 clusters (three layers of two, four, and two MoOn octahedra) are distinguishable from the [Mo8O26](4-) cluster formed in acidic solutions by two displaced MoOn octahedra implicating three kinetically labile terminal ligands. Stabilization in the covalent Mo-8 cluster is achieved by Mo bonding to His alpha 156-N-epsilon 2 and Glu alpha 129-O-epsilon 1. The absence of covalent protein interactions in the noncovalent Mo-8 cluster is compensated by a more extended hydrogen-bond network involving three pronounced histidines. One displaced MoOn octahedron might serve as nucleation site for an inhomogeneous Mo5-7 cluster largely surrounded by bulk solvent. In the Mo-3 cluster located on the 3-fold axis, the three accurately positioned His140-N-epsilon 2 atoms of the alpha subunits coordinate to the Mo atoms. The formed polyoxomolybdate clusters of MoSto, not detectable in bulk solvent, are the result of an interplay between self- and protein-driven assembly processes that unite inorganic supramolecular and protein chemistry in a host-guest system. Template, nucleation/protection, and catalyst functions of the polypeptide as well as perspectives for designing new clusters are discussed.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Kowalewski B, Poppe J, Demmer U, et al. Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters. Journal of the American Chemical Society. 2012;134(23):9768-9774.
Kowalewski, B., Poppe, J., Demmer, U., Warkentin, E., Dierks, T., Ermler, U., & Schneider, K. (2012). Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters. Journal of the American Chemical Society, 134(23), 9768-9774.
Kowalewski, B., Poppe, J., Demmer, U., Warkentin, E., Dierks, T., Ermler, U., and Schneider, K. (2012). Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters. Journal of the American Chemical Society 134, 9768-9774.
Kowalewski, B., et al., 2012. Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters. Journal of the American Chemical Society, 134(23), p 9768-9774.
B. Kowalewski, et al., “Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters”, Journal of the American Chemical Society, vol. 134, 2012, pp. 9768-9774.
Kowalewski, B., Poppe, J., Demmer, U., Warkentin, E., Dierks, T., Ermler, U., Schneider, K.: Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters. Journal of the American Chemical Society. 134, 9768-9774 (2012).
Kowalewski, Björn, Poppe, Juliane, Demmer, Ulrike, Warkentin, Eberhard, Dierks, Thomas, Ermler, Ulrich, and Schneider, Klaus. “Nature's Polyoxometalate Chemistry: X-ray Structure of the Mo Storage Protein Loaded with Discrete Polynuclear Mo-O Clusters”. Journal of the American Chemical Society 134.23 (2012): 9768-9774.
This data publication is cited in the following publications:
This publication cites the following data publications:

8 Citations in Europe PMC

Data provided by Europe PubMed Central.

Porous capsules with a large number of active sites: nucleation/growth under confined conditions.
Garai S, Rubcic M, Bogge H, Gouzerh P, Muller A., Chemistry 21(11), 2015
PMID: 25653204
Hen egg-white lysozyme crystallisation: protein stacking and structure stability enhanced by a Tellurium(VI)-centred polyoxotungstate.
Bijelic A, Molitor C, Mauracher SG, Al-Oweini R, Kortz U, Rompel A., Chembiochem 16(2), 2015
PMID: 25521080
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., J. Inorg. Biochem. 138(), 2014
PMID: 24945101
High-resolution molybdenum K-edge X-ray absorption spectroscopy analyzed with time-dependent density functional theory.
Lima FA, Bjornsson R, Weyhermuller T, Chandrasekaran P, Glatzel P, Neese F, DeBeer S., Phys Chem Chem Phys 15(48), 2013
PMID: 24197060

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 22612644
PubMed | Europe PMC

Search this title in

Google Scholar