Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center

Glaser T, Liratzis I, Kataeva O, Fröhlich R, Piacenza M, Grimme S (2006)
CHEMICAL COMMUNICATIONS (9): 1024-1026.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Glaser, ThorstenUniBi; Liratzis, I; Kataeva, O; Fröhlich, R; Piacenza, M; Grimme, S
Einrichtung
Fakultät für Chemie > Anorganische Chemie I
Abstract / Bemerkung
Two hydrogen-bonds from geometrically constrained OH groups to coordinated oxygen donors shift the reduction potential of a Cu-II complex by + 270 mV as compared to the structurally analogous reference complex missing the OH groups.
Erscheinungsjahr
2006
Zeitschriftentitel
CHEMICAL COMMUNICATIONS
Ausgabe
9
Seite(n)
1024-1026
ISSN
1359-7345
eISSN
1364-548X
Page URI
https://pub.uni-bielefeld.de/record/1600115

Zitieren

Glaser T, Liratzis I, Kataeva O, Fröhlich R, Piacenza M, Grimme S. Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center. CHEMICAL COMMUNICATIONS. 2006;(9):1024-1026.
Glaser, T., Liratzis, I., Kataeva, O., Fröhlich, R., Piacenza, M., & Grimme, S. (2006). Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center. CHEMICAL COMMUNICATIONS(9), 1024-1026. https://doi.org/10.1039/b517340j
Glaser, Thorsten, Liratzis, I, Kataeva, O, Fröhlich, R, Piacenza, M, and Grimme, S. 2006. “Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center”. CHEMICAL COMMUNICATIONS, no. 9: 1024-1026.
Glaser, T., Liratzis, I., Kataeva, O., Fröhlich, R., Piacenza, M., and Grimme, S. (2006). Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center. CHEMICAL COMMUNICATIONS, 1024-1026.
Glaser, T., et al., 2006. Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center. CHEMICAL COMMUNICATIONS, (9), p 1024-1026.
T. Glaser, et al., “Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center”, CHEMICAL COMMUNICATIONS, 2006, pp. 1024-1026.
Glaser, T., Liratzis, I., Kataeva, O., Fröhlich, R., Piacenza, M., Grimme, S.: Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center. CHEMICAL COMMUNICATIONS. 1024-1026 (2006).
Glaser, Thorsten, Liratzis, I, Kataeva, O, Fröhlich, R, Piacenza, M, and Grimme, S. “Direct influence of hydrogen-bonding on the reduction potential of a Cu-II center”. CHEMICAL COMMUNICATIONS 9 (2006): 1024-1026.

1 Zitation in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Design and synthesis of a dinucleating ligand system with varying terminal donor functions that provides no bridging donor and its application to the synthesis of a series of Fe(III)-μ-O-Fe(III) complexes.
Strautmann JB, Dammers S, Limpke T, Parthier J, Zimmermann TP, Walleck S, Heinze-Brückner G, Stammler A, Bögge H, Glaser T., Dalton Trans 45(8), 2016
PMID: 26791942

27 References

Daten bereitgestellt von Europe PubMed Central.

Principles of mononucleating and binucleating ligand design.
Gavrilova AL, Bosnich B., Chem. Rev. 104(2), 2004
PMID: 14871128
Bioinspired hydrogen bond motifs in ligand design: the role of noncovalent interactions in metal ion mediated activation of dioxygen.
Borovik AS., Acc. Chem. Res. 38(1), 2005
PMID: 15654737
Combined spectroscopic/computational studies on Fe- and Mn-dependent superoxide dismutases: insights into second-sphere tuning of active site properties.
Jackson TA, Brunold TC., Acc. Chem. Res. 37(7), 2004
PMID: 15260508

Solomon, Coord. Chem. Rev. 200–202(), 2000
Protein Control of Redox Potentials of Ironminus signSulfur Proteins.
Stephens PJ, Jollie DR, Warshel A., Chem. Rev. 96(7), 1996
PMID: 11848834
NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein.
Adman E, Watenpaugh KD, Jensen LH., Proc. Natl. Acad. Sci. U.S.A. 72(12), 1975
PMID: 1061073

Low, J. Am. Chem. Soc. 122(), 2000
Protein effects on the electronic structure of the [Fe4S4]2+ cluster in ferredoxin and HiPIP.
Glaser T, Bertini I, Moura JJ, Hedman B, Hodgson KO, Solomon EI., J. Am. Chem. Soc. 123(20), 2001
PMID: 11457306
Determinants of the relative reduction potentials of type-1 copper sites in proteins.
Li H, Webb SP, Ivanic J, Jensen JH., J. Am. Chem. Soc. 126(25), 2004
PMID: 15212551
Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins.
Solomon EI, Szilagyi RK, DeBeer George S, Basumallick L., Chem. Rev. 104(2), 2004
PMID: 14871131

Walters, Inorg. Chem. 30(), 1991
Structure and Properties of [Fe(4)S(4){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-) and [Fe(2)S(2){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-): Protection of the Fe-S Bond by Double NH.S Hydrogen Bonds.
Ueyama N, Yamada Y, Okamura Ta , Kimura S, Nakamura A., Inorg Chem 35(22), 1996
PMID: 11666795
Novel Rubredoxin Model Tetrathiolato Iron(II) and Cobalt(II) Complexes Containing Intramolecular Single and Double NH.S Hydrogen Bonds.
Okamura Ta , Takamizawa S, Ueyama N, Nakamura A., Inorg Chem 37(1), 1998
PMID: 11670255
N-H...S hydrogen bonds in a ferredoxin model.
Walters MA, Roche CL, Rheingold AL, Kassel SW., Inorg Chem 44(11), 2005
PMID: 15907101
Direct measurement of the hydrogen-bonding effect on the intrinsic redox potentials of [4Fe-4S] cubane complexes.
Yang X, Niu S, Ichiye T, Wang LS., J. Am. Chem. Soc. 126(48), 2004
PMID: 15571403

Gebhard, J. Am. Chem. Soc. 112(), 1990

Gebhard, J. Am. Chem. Soc. 113(), 1991

Sträter, Angew. Chem., Int. Ed. Engl. 35(), 1996

DiMauro, Organometallics 21(), 2002

Zhang, J. Am. Chem. Soc. 112(), 1990

Irie, Tetrahedron Lett. 31(), 1990
Asymmetric catalysis of epoxide ring-opening reactions.
Jacobsen EN., Acc. Chem. Res. 33(6), 2000
PMID: 10891060

Glaser, Dalton Trans. (), 2005

Bhadbhade, Inorg. Chem. 32(), 1993

Becke, J. Chem. Phys. 98(), 1993

Lee, Phys. Rev. B: Condens. Matter 37(), 1988

Huber, J. Chem. Phys. 100(), 1994
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 16491197
PubMed | Europe PMC

Suchen in

Google Scholar