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287 Aktuelle Fachpublikationen zum Thema Addition

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Investigating the in Vitro Thermal Stability and Conformational Flexibility of Estrogen Receptors as Potential Key Factors of Their in Vivo Activity

18.06.2015 | Adélaïde Le Grand; Gwenaëlle André-Leroux; Gaëlle Marteil; Hélène Duval; Olivier Sire; Véronique Le Tilly, Biochemistry, 2015

Among hormone-inducible transcription factors, estrogen receptors (ERs) play important roles in tissue growth and differentiation, via either direct or indirect binding, in the nucleus, to specific DNA targets called estrogen responsive elements (EREs), or through nongenomic pathways. In humans, ...


Cation-Specific Conformations in a Dual-Function Ion-Pumping Microbial Rhodopsin

17.06.2015 | Giordano F. Z. da Silva; Brandon R. Goblirsch; Ah-Lim Tsai; John L. Spudich, Biochemistry, 2015

A recently discovered rhodopsin ion pump (DeNaR, also known as KR2) in the marine bacterium Dokdonia eikasta uses light to pump protons or sodium ions from the cell depending on the ionic composition of the medium. In cells suspended in a KCl solution, DeNaR functions as a light-driven proton ...


The Human Iron–Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules

12.06.2015 | Nicholas G. Fox; Mrinmoy Chakrabarti; Sean P. McCormick; Paul A. Lindahl; David P. Barondeau, Biochemistry, 2015

Iron–sulfur (Fe–S) clusters are essential protein cofactors for most life forms. In human mitochondria, the core Fe–S biosynthetic enzymatic complex (called SDUF) consists of NFS1, ISD11, ISCU2, and frataxin (FXN) protein components. Few mechanistic details about how this complex synthesizes Fe–S ...


Correlations between the Electronic Properties of Shewanella oneidensis Cytochrome c Nitrite Reductase (ccNiR) and Its Structure: Effects of Heme Oxidation State and Active Site Ligation

12.06.2015 | Natalia Stein; Daniel Love; Evan T. Judd; Sean J. Elliott; Brian Bennett; A. Andrew Pacheco, Biochemistry, 2015

The electrochemical properties of Shewanella oneidensis cytochrome c nitrite reductase (ccNiR), a homodimer that contains five hemes per protomer, were investigated by UV–visible and electron paramagnetic resonance (EPR) spectropotentiometries. Global analysis of the UV–vis spectropotentiometric ...


HYSCORE Analysis of the Effects of Substrates on Coordination of Water to the Active Site Iron in Tyrosine Hydroxylase

09.06.2015 | John McCracken; Bekir E. Eser; Donald Mannikko; Matthew D. Krzyaniak; Paul F. Fitzpatrick, Biochemistry, 2015

Tyrosine hydroxylase is a mononuclear non-heme iron monooxygenase found in the central nervous system that catalyzes the hydroxylation of tyrosine to yield l-3,4-dihydroxyphenylalanine, the rate-limiting step in the biosynthesis of catecholamine neurotransmitters. Catalysis requires the binding ...


Mechanistic Studies of the Radical S-Adenosyl-l-methionine Enzyme 4-Demethylwyosine Synthase Reveal the Site of Hydrogen Atom Abstraction

08.06.2015 | Anthony P. Young; Vahe Bandarian, Biochemistry, 2015

TYW1 catalyzes the formation of 4-demethylwyosine via the condensation of N-methylguanosine (m1G) with carbons 2 and 3 of pyruvate. In this study, labeled transfer ribonucleic acid (tRNA) and pyruvate were utilized to determine the site of hydrogen atom abstraction and regiochemistry of the ...


Crystal Structure and Product Analysis of an Archaeal myo-Inositol Kinase Reveal Substrate Recognition Mode and 3-OH Phosphorylation

29.05.2015 | Ryuhei Nagata; Masahiro Fujihashi; Takaaki Sato; Haruyuki Atomi; Kunio Miki, Biochemistry, 2015

The TK2285 protein from Thermococcus kodakarensis was recently characterized as an enzyme catalyzing the phosphorylation of myo-inositol. Only two myo-inositol kinases have been identified so far, the TK2285 protein and Lpa3 from Zea mays, both of which belong to the ribokinase family. In either ...


Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus

21.05.2015 | Joseph E. Sanchez; Phillip G. Gross; Russell W. Goetze; Richard M. Walsh, Jr.; William B. Peeples; Zachary A. Wood, Biochemistry, 2015

Ketopantoate reductase (KPR) catalyzes the NADPH-dependent production of pantoate, an essential precursor in the biosynthesis of coenzyme A. Previous structural studies have been limited to Escherichia coli KPR, a monomeric enzyme that follows a sequential ordered mechanism. Here we report the ...


Subunit Interactions within the Carbon–Phosphorus Lyase Complex from Escherichia coli

19.05.2015 | Zhongjie Ren; Soumya Ranganathan; Nathanael F. Zinnel; William K. Russell; David H. Russell; Frank M. Raushel, Biochemistry, 2015

Phosphonates are a large class of organophosphorus compounds with a characteristic carbon–phosphorus bond. The genes responsible for phosphonate utilization in Gram-negative bacteria are arranged in an operon of 14 genes. The carbon–phosphorus lyase complex, encoded by the genes phnGHIJKLM, ...


Cryo-Electron Microscopy and the Amazing Race to Atomic Resolution

14.05.2015 | Elad Binshtein; Melanie D. Ohi, Biochemistry, 2015

Cryo-electron microscopy (cryo-EM), the structural analysis of samples embedded in vitreous ice, is a powerful approach for determining three-dimensional (3D) structures of biological specimens. Over the past two decades, this technique has been used to successfully calculate subnanometer ...


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