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High-resolution crystal structures of a "half sandwich"-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K
Chiniadis, L., Bratsos, I., Bethanis, K., Karpusas, M., Giastas, P., & Papakyriakou, A. (2020). High-resolution crystal structures of a "half sandwich"-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K. Journal of Biological Inorganic Chemistry, 25, 635-645. https://doi.org/10.1007/s00775-020-01786-z
The <em>Bacillus anthracis</em> class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron
Grāve, K., Griese, J. J., Berggren, G., Bennett, M. D., & Högbom, M. (2020). The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron. Journal of Biological Inorganic Chemistry, 25, 571-582. https://doi.org/10.1007/s00775-020-01782-3
Distinctive structural properties of THB11, a pentacoordinate <em>Chlamydomonas reinhardtii</em> truncated hemoglobin with N- and C-terminal extensions
Huwald, D., Duda, S., Gasper, R., Olieric, V., Hofmann, E., & Hemschemeier, A. (2020). Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions. Journal of Biological Inorganic Chemistry, 25, 267-283. https://doi.org/10.1007/s00775-020-01759-2
Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase
Griese, J. J., Kositzki, R., Haumann, M., & Högbom, M. (2019). Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase. Journal of Biological Inorganic Chemistry, 24(2), 211-221. https://doi.org/10.1007/s00775-019-01639-4
Redox-induced structural changes in the di-iron and di-manganese forms of <em>Bacillus anthracis</em> ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access
Grāve, K., Lambert, W., Berggren, G., Griese, J. J., Bennett, M. D., Logan, D. T., & Högbom, M. (2019). Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access. Journal of Biological Inorganic Chemistry, 24(6), 849-861. https://doi.org/10.1007/s00775-019-01703-z
Metal binding to the amyloid-β peptides in the presence of biomembranes: potential mechanisms of cell toxicity
Wärmländer, S. K. T. S., Österlund, N., Wallin, C., Wu, J., Luo, J., Tiiman, A., … Gräslund, A. (2019). Metal binding to the amyloid-β peptides in the presence of biomembranes: potential mechanisms of cell toxicity. Journal of Biological Inorganic Chemistry, 24(8), 1189-1196. https://doi.org/10.1007/s00775-019-01723-9
Ether cross-link formation in the R2-like ligand-binding oxidase
Griese, J. J., Branca, R. M. M., Srinivas, V., & Högbom, M. (2018). Ether cross-link formation in the R2-like ligand-binding oxidase. Journal of Biological Inorganic Chemistry, 23(6), 879-886. https://doi.org/10.1007/s00775-018-1583-3
Crystal structure of VnfH, the iron protein component of vanadium nitrogenase
Rohde, M., Trncik, C., Sippel, D., Gerhardt, S., & Einsle, O. (2018). Crystal structure of VnfH, the iron protein component of vanadium nitrogenase. Journal of Biological Inorganic Chemistry, 23(7), 1049-1056. https://doi.org/10.1007/s00775-018-1602-4
Insights into the structure-activity relationships of chiral 1,2-diaminophenylalkane platinum(II) anticancer derivatives
Berger, G., Fusaro, L., Luhmer, M., Czapla-Masztafiak, J., Lipiec, E., Szlachetko, J., … Bombard, S. (2015). Insights into the structure-activity relationships of chiral 1,2-diaminophenylalkane platinum(II) anticancer derivatives. Journal of Biological Inorganic Chemistry, 20(5), 841-853. https://doi.org/10.1007/s00775-015-1270-6
The discovery of Mo(III) in FeMoco: Reuniting enzyme and model chemistry
Bjornsson, R., Neese, F., Schrock, R. R., Einsle, O., & Debeer, S. (2015). The discovery of Mo(III) in FeMoco: Reuniting enzyme and model chemistry. Journal of Biological Inorganic Chemistry, 20(2), 447-460. https://doi.org/10.1007/s00775-014-1230-6
Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'
Ghafoor, D. D., Kekilli, D., Abdullah, G. H., Dworkowski, F. S. N., Hassan, H. G., Wilson, M. T., … Hough, M. A. (2015). Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'. Journal of Biological Inorganic Chemistry, 20(6), 949-956. https://doi.org/10.1007/s00775-015-1278-y
Conformational control of the binding of diatomic gases to cytochrome c′
Manole, A., Kekilli, D., Svistunenko, D. A., Wilson, M. T., Dobbin, P. S., & Hough, M. A. (2015). Conformational control of the binding of diatomic gases to cytochrome c′. Journal of Biological Inorganic Chemistry, 20(4), 675-686. https://doi.org/10.1007/s00775-015-1253-7
Structural characterization of metal binding to a cold-adapted frataxin
Noguera, M. E., Roman, E. A., Rigal, J. B., Cousido-Siah, A., Mitschler, A., Podjarny, A., & Santos, J. (2015). Structural characterization of metal binding to a cold-adapted frataxin. Journal of Biological Inorganic Chemistry, 20(4), 653-664. https://doi.org/10.1007/s00775-015-1251-9
Nitrogenase FeMo cofactor: An atomic structure in three simple steps
Einsle, O. (2014). Nitrogenase FeMo cofactor: An atomic structure in three simple steps. Journal of Biological Inorganic Chemistry, 19(6), 737-745. https://doi.org/10.1007/s00775-014-1116-7
A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase
Fielding, A. J., Kovaleva, E. G., Farquhar, E. R., Lipscomb, J. D., & Que Jr., L. (2011). A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase. Journal of Biological Inorganic Chemistry, 16(2), 341-355. https://doi.org/10.1007/s00775-010-0732-0
Structure at 1.0 Å resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of <em>Rhodothermus marinus</em>
Stelter, M., Melo, A. M. P., Hreggvidsson, G. O., Hjorleifsdottir, S., Saraiva, L. M., Teixeira, M., & Archer, M. (2010). Structure at 1.0 Å resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus. Journal of Biological Inorganic Chemistry, 15(3), 303-313. https://doi.org/10.1007/s00775-009-0603-8
Distorted octahedral coordination of tungstate in a subfamily of specific binding proteins
Hollenstein, K., Comellas-Bigler, M., Bevers, L. E., Feiters, M. C., Meyer-Klaucke, W., Hagedoorn, P. L., & Locher, K. P. (2009). Distorted octahedral coordination of tungstate in a subfamily of specific binding proteins. Journal of Biological Inorganic Chemistry, 14(5), 663-672. https://doi.org/10.1007/s00775-009-0479-7