Ryde U - Search Results

1

Why does sulfite reductase employ siroheme?

Brânzanic AMV, Ryde U, Silaghi-Dumitrescu R. Brânzanic AMV, et al. Among authors: ryde u. Chem Commun (Camb). 2019 Dec 4;55(93):14047-14049. doi: 10.1039/c9cc05271b. Epub 2019 Nov 6. Chem Commun (Camb). 2019. PMID: 31690895

2

Importance of the iron-sulfur component and of the siroheme modification in the resting state of sulfite reductase.

Brânzanic AMV, Ryde U, Silaghi-Dumitrescu R. Brânzanic AMV, et al. Among authors: ryde u. J Inorg Biochem. 2020 Feb;203:110928. doi: 10.1016/j.jinorgbio.2019.110928. Epub 2019 Nov 18. J Inorg Biochem. 2020. PMID: 31756559

3

A quantum-mechanical study of the reaction mechanism of sulfite oxidase.

van Severen MC, Andrejić M, Li J, Starke K, Mata RA, Nordlander E, Ryde U. van Severen MC, et al. Among authors: ryde u. J Biol Inorg Chem. 2014 Oct;19(7):1165-79. doi: 10.1007/s00775-014-1172-z. Epub 2014 Jun 24. J Biol Inorg Chem. 2014. PMID: 24957901

4

Geometry, reduction potential, and reorganization energy of the binuclear Cu(A) site, studied by density functional theory.

Olsson MH, Ryde U. Olsson MH, et al. Among authors: ryde u. J Am Chem Soc. 2001 Aug 15;123(32):7866-76. doi: 10.1021/ja010315u. J Am Chem Soc. 2001. PMID: 11493060

5

Ligand-Binding Affinity Estimates Supported by Quantum-Mechanical Methods.

Ryde U, Söderhjelm P. Ryde U, et al. Chem Rev. 2016 May 11;116(9):5520-66. doi: 10.1021/acs.chemrev.5b00630. Epub 2016 Apr 14. Chem Rev. 2016. PMID: 27077817 Free article. Review.

6

Effect of the protein ligand in DMSO reductase studied by computational methods.

Dong G, Ryde U. Dong G, et al. Among authors: ryde u. J Inorg Biochem. 2017 Jun;171:45-51. doi: 10.1016/j.jinorgbio.2017.03.004. Epub 2017 Mar 21. J Inorg Biochem. 2017. PMID: 28364618

7

N₂ binding to the E₀-E₄ states of nitrogenase.

Jiang H, Ryde U. Jiang H, et al. Among authors: ryde u. Dalton Trans. 2023 Jul 4;52(26):9104-9120. doi: 10.1039/d3dt00648d. Dalton Trans. 2023. PMID: 37338432

8

Identification of the peroxy adduct in multicopper oxidases by a combination of computational chemistry and extended X-ray absorption fine-structure measurements.

Ryde U, Hsiao YW, Rulísek L, Solomon EI. Ryde U, et al. J Am Chem Soc. 2007 Jan 31;129(4):726-7. doi: 10.1021/ja062954g. J Am Chem Soc. 2007. PMID: 17243785 No abstract available.

9

Reorganization energy for internal electron transfer in multicopper oxidases.

Hu L, Farrokhnia M, Heimdal J, Shleev S, Rulíšek L, Ryde U. Hu L, et al. Among authors: ryde u. J Phys Chem B. 2011 Nov 17;115(45):13111-26. doi: 10.1021/jp205897z. Epub 2011 Oct 19. J Phys Chem B. 2011. PMID: 21955325

10

Comparison of the active-site design of molybdenum oxo-transfer enzymes by quantum mechanical calculations.

Li J, Ryde U. Li J, et al. Among authors: ryde u. Inorg Chem. 2014 Nov 17;53(22):11913-24. doi: 10.1021/ic5010837. Epub 2014 Nov 5. Inorg Chem. 2014. PMID: 25372012

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