Results 21 to 30 of about 21,893 (312)

Redox-controlled reorganization and flavin strain within the ribonucleotide reductase R2b–NrdI complex monitored by serial femtosecond crystallography

eLife, 2022
Redox reactions are central to biochemistry and are both controlled by and induce protein structural changes. Here, we describe structural rearrangements and crosstalk within the Bacillus cereus ribonucleotide reductase R2b–NrdI complex, a di-metal ...
Juliane John, Oskar Aurelius, Vivek Srinivas, Patricia Saura, In-Sik Kim, Asmit Bhowmick, Philipp S Simon, Medhanjali Dasgupta, Cindy Pham, Sheraz Gul, Kyle D Sutherlin, Pierre Aller, Agata Butryn, Allen M Orville, Mun Hon Cheah, Shigeki Owada, Kensuke Tono, Franklin D Fuller, Alexander Batyuk, Aaron S Brewster, Nicholas K Sauter, Vittal K Yachandra, Junko Yano, Ville RI Kaila, Jan Kern, Hugo Lebrette, Martin Högbom   +26 more
doaj   +1 more source

Metalloproteins in the Biology of Heterocysts [PDF]

Life, 2019
Cyanobacteria are photoautotrophic microorganisms present in almost all ecologically niches on Earth. They exist as single-cell or filamentous forms and the latter often contain specialized cells for N2 fixation known as heterocysts. Heterocysts arise from photosynthetic active vegetative cells by multiple morphological and physiological rearrangements
Pernil, Rafael, Schleiff, Enrico
openaire   +6 more sources

Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone. [PDF]

PLoS ONE, 2012
Molecular recognition is central to all biological processes. Understanding the key role played by dedicated chaperones in metalloprotein folding and assembly requires the knowledge of their conformational ensembles.
Magali Lorenzi, Léa Sylvi, Guillaume Gerbaud, Elisabetta Mileo, Frédéric Halgand, Anne Walburger, Hervé Vezin, Valérie Belle, Bruno Guigliarelli, Axel Magalon   +9 more
doaj   +1 more source

Combinatorial targeting of G‐protein‐coupled bile acid receptor 1 and cysteinyl leukotriene receptor 1 reveals a mechanistic role for bile acids and leukotrienes in drug‐induced liver injury

Hepatology, EarlyView., 2022
CHIN117 is a dual cysteinyl leukotriene receptor 1 (CYSLTR1) antagonist and G‐protein‐coupled bile acid receptor 1 (GPBAR1) agonist. In the liver, GPBAR1 and CYSLTR1 are coexpressed by liver sinusoidal endothelial cells (LSECs), HSCs, circulating monocytes/macrophages, and liver resident macrophages (Kupffer cells).
Michele Biagioli, Silvia Marchianò, Cristina di Giorgio, Rosalinda Roselli, Martina Bordoni, Rachele Bellini, Bianca Fiorillo, Valentina Sepe, Bruno Catalanotti, Chiara Cassiano, Maria Chiara Monti, Eleonora Distrutti, Angela Zampella, Stefano Fiorucci   +13 more
wiley   +1 more source

Inter-Subunit Dynamics Controls Tunnel Formation During the Oxygenation Process in Hemocyanin Hexamers

Frontiers in Molecular Biosciences, 2021
Hemocyanin from horseshoe crab in its active form is a homo-hexameric protein. It exists in open and closed conformations when transitioning between deoxygenated and oxygenated states.
Khair Bux, Xiayu Shen, Muhammad Tariq, Junqi Yin, Syed Tarique Moin, Debsindhu Bhowmik, Shozeb Haider   +6 more
doaj   +1 more source

Functional Expression and Characterization of a Panel of Cobalt and Iron-Dependent Nitrile Hydratases

Molecules, 2020
Nitrile hydratases (NHase) catalyze the hydration of nitriles to the corresponding amides. We report on the heterologous expression of various nitrile hydratases.
Birgit Grill, Maximilian Glänzer, Helmut Schwab, Kerstin Steiner, Daniel Pienaar, Dean Brady, Kai Donsbach, Margit Winkler   +7 more
doaj   +1 more source

Pico-meter resolution structure of the coordination sphere in the metal-binding site in a metalloprotein by NMR.

Journal of the American Chemical Society, 2020
Most of our understanding of chemistry derives from atomic-level structures obtained with single crystal X-ray diffraction. Metal centers in X-ray structures of small organometallic or coordination complexes are often extremely well defined, with errors ...
A. Bertarello, L. Benda, K. Sanders, A. J. Pell, Michael J Knight, Vladimir Pelmenschikov, L. Gonnelli, I. Felli, M. Kaupp, L. Emsley, R. Pierattelli, G. Pintacuda   +11 more
semanticscholar   +1 more source

Computational Treatment of Metalloproteins [PDF]

The Journal of Physical Chemistry B, 2015
Metalloproteins present a considerable challenge for modeling, especially when the starting point is far from thermodynamic equilibrium. Examples include formidable problems such as metalloprotein folding and structure prediction upon metal addition, removal, or even just replacement; metalloenzyme design, where stabilization of a transition state of ...
Nechay, Michael R, Valdez, Crystal E, Alexandrova, Anastassia N   +2 more
openaire   +5 more sources

Microcontact printing of metalloproteins [PDF]

Synthetic Metals, 2005
The morphological investigation by scanning probes techniques, and especially Atomic Force Microscopy (AFM) allow to measure the surface roughness of immobilized proteins with unequalled vertical spatial resolution. This is particularly important, since the biological role of proteins is closely related to their physiological folding architectures.
BIASCO, Adriana Lucia Angela, PISIGNANO, Dario, B. KREBS, CINGOLANI, Roberto, RINALDI, Rosaria   +4 more
openaire   +5 more sources

Probing a Complex of Cytochromecand Cardiolipin by Magnetic Circular Dichroism Spectroscopy: Implications for the Initial Events in Apoptosis [PDF]

, 2011
Oxidation of cardiolipin (CL) by its complex with cytochrome c (cyt c) plays a crucial role in triggering apoptosis. Through a combination of magnetic circular dichroism spectroscopy and potentiometric titrations, we show that both the ferric and ferrous
Armstrong F. A., Barker P. D., Basova L. V., Battistuzzi G., Battistuzzi G., Belikova N. A., Belikova N. A., Bradley J. M., Bushnell G. W., Cheesman M. R., Cheesman M. R., Ferrer J. C., Foote N., Gadsby P. M. A., Gadsby P. M. A., Gary Silkstone, Hendriks J. H. M., Jing W. G., Julea N. Butt, Justin M. Bradley, Kagan V. E., Kagan V. E., Kalanxhi E., Kapetanaki S. M., Kapralov A. A., Marritt S. J., Michael T. Wilson, Millis K. K., Myles R. Cheesman, Nantes I. L., Oganesyan V. S., Petrovic J., Pettigrew G. W., Pond A. E., Rawlings J., Rigby S. E. J., Rytomaa M., Salamon Z., Sinibaldi F., Sutherland J., Tezcan F. A., Wackerbarth H., Zucchi M. R.   +42 more
core   +1 more source