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On the nucleus structure and activity of comet 67P/Churyumov-Gerasimenko
Images from the OSIRIS scientific imaging system onboard Rosetta show that the nucleus of 67P/Churyumov-Gerasimenko consists of two lobes connected by a short neck, which raises the question of whether the two Lobes represent a contact binary formed 4.5 billion years ago, or a single body where a gap has evolved via mass loss.
Dust measurements in the coma of comet 67P/Churyumov-Gerasimenko inbound to the Sun
The largest orbiting clumps are meter-sized, confirming the dust/gas ratio of 3 inferred at perihelion from models of dust comae and trails.
Metal ions in biological catalysis: from enzyme databases to general principles
- C. Andreini, I. Bertini, G. Cavallaro, Gemma L. Holliday, J. Thornton
- Chemistry, MedicineJBIC Journal of Biological Inorganic Chemistry
- 5 July 2008
Redox-inert metal ions are used in enzymes to stabilize negative charges and to activate substrates by virtue of their Lewis acid properties, whereas redox-active metal ions can be used both as Lewis acids and as redox centres.
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria
- L. Banci, I. Bertini, +6 authors K. Tokatlidis
- Biology, MedicineNature Structural &Molecular Biology
- 1 February 2009
MIA40 represents a thioredoxin-unrelated, minimal oxidoreductase, with a facile CPC redox active site that ensures its catalytic function in oxidative folding in mitochondria.
Solution NMR of Paramagnetic Molecules: Applications to metallobiomolecules and models
Selected Contents. Introduction. The hyperfine shift. Relaxation. Chemical exchange, chemical equilibria and dynamics. Transition metal ions: shift and relaxation. Magnetic coupled systems. Nuclear…
Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake.
- D. Achila, L. Banci, I. Bertini, J. Bunce, S. Ciofi‐Baffoni, D. Huffman
- Chemistry, MedicineProceedings of the National Academy of Sciences…
- 11 April 2006
Human Wilson protein is a copper-transporting ATPase located in the secretory pathway possessing six N-terminal metal-binding domains, which are suggested to be two acceptors of Cu(I) from HAH1, which then somehow route copper to WLN5-6, before the ATP-driven transport of copper across the vesicular membrane.
Counting the zinc-proteins encoded in the human genome.
The present bioinformatic research proposes a strategy to answer the question of how many and which proteins encoded in the human genome may require zinc for their physiological function by a combination of approaches, which include searching in the proteome for the zinc-binding patterns that are obtained from all available X-ray data.
Handbook on Metalloproteins
Interaction of sodium and potassium with proteins structure and function of sodium and potassium channel proteins in membranes magnesium-activated enzyme systems calcium and its enzymes vanadium in…
Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer
- L. Banci, I. Bertini, S. Ciofi‐Baffoni, T. Hadjiloi, M. Martinelli, P. Palumaa
- Chemistry, MedicineProceedings of the National Academy of Sciences
- 13 May 2008
It is shown here that Cu(I)HCox172S-S, i.e., the copper-loaded form of the protein, can transfer simultaneously copper( I) and two electrons to the human cochaperone Sco1 (HSco1) in the oxidized state, with its metal-binding cysteines forming a disulfide bond.