Results 221 to 230 of about 22,558 (250)
Some of the next articles are maybe not open access.
Metalloproteins in the evolution of photosynthesis
Biosystems, 1981Certain metalloproteins are common to all photosynthetic electron transfer chains. These include soluble proteins such as ferredoxins and cytochromes of the c2 type, and membrane-bound components such as cytochrome b, c1 and the Rieske iron-sulphur protein.
K.K. Rao, D.O. Hall, R. Cammack
openaire +3 more sources
Current Opinion in Biotechnology, 1996
The rational design of novel proteins offers a new method of studying structure and function, and makes possible the construction of new biomaterials. The richness of metal chemistry, the relative ease of creating stable complexes, and the remarkable degree of subtle, highly specific control of reactivity imposed by the protein matrix upon the metal ...
openaire +2 more sources
The rational design of novel proteins offers a new method of studying structure and function, and makes possible the construction of new biomaterials. The richness of metal chemistry, the relative ease of creating stable complexes, and the remarkable degree of subtle, highly specific control of reactivity imposed by the protein matrix upon the metal ...
openaire +2 more sources
2013
Paramagnetic metalloproteins are proteins containing one or more paramagnetic metal ions, which are characterized by the presence of at least one unpaired electron. As in every molecule, unpaired electrons sizably perturb the NMR parameters relative to the protein nuclei, changing their relaxation, chemical shift, and motional averaging so that ...
BERTINI, IVANO, PARIGI, GIACOMO
openaire +2 more sources
Paramagnetic metalloproteins are proteins containing one or more paramagnetic metal ions, which are characterized by the presence of at least one unpaired electron. As in every molecule, unpaired electrons sizably perturb the NMR parameters relative to the protein nuclei, changing their relaxation, chemical shift, and motional averaging so that ...
BERTINI, IVANO, PARIGI, GIACOMO
openaire +2 more sources
Metalloproteins and metal sensing
Nature, 2009Almost half of all enzymes must associate with a particular metal to function. An ambition is to understand why each metal-protein partnership arose and how it is maintained. Metal availability provides part of the explanation, and has changed over geological time and varies between habitats but is held within vital limits in cells.
Nigel J. Robinson +3 more
openaire +3 more sources
ChemInform, 1988
Publisher Summary Nickel has long been suspected to be an essential trace element for living organisms, but the identification of its functions in molecular terms is relatively recent. The first nickel protein to be identified was urease (urea ammonia hydrolase) from jack bean.
openaire +3 more sources
Publisher Summary Nickel has long been suspected to be an essential trace element for living organisms, but the identification of its functions in molecular terms is relatively recent. The first nickel protein to be identified was urease (urea ammonia hydrolase) from jack bean.
openaire +3 more sources
EXAFS: a probe for metalloproteins
Nature, 1990X-ray absorption spectroscopy provides a method for studying the local environment around a metal atom in a protein.
openaire +3 more sources
2001
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 proteins and enzymes are there proteins containing chromium?
Ivano Bertini +2 more
openaire +2 more sources
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 proteins and enzymes are there proteins containing chromium?
Ivano Bertini +2 more
openaire +2 more sources
FTIR Spectroscopy of Metalloproteins
2014Absorption of infrared radiation by proteins gives important information about their structure and function. The most intense infrared bands correspond to the overlap of all the peptide bond absorption. Additionally, in many metalloproteins their prosthetic groups have intrinsic ligands or bind substrates/inhibitors that absorb intensively in the ...
Antonio L. De Lacey +2 more
openaire +3 more sources
A supramolecular assembly enables discrimination between metalloproteins and non-metalloproteins
Chemical Communications, 2018A supramolecular assembly yields turn-on fluorescence response for non-metalloproteins and turn-off response for metalloproteins.
Aafrin M. Pettiwala +2 more
openaire +3 more sources
2006
Volume 1 IRON Heme Proteins: Oxygen Storage and Oxygen Transport Proteins Heme Proteins: Cytochromes Heme Proteins: Cytochrome Peroxidases Heme Proteins: Cytochrome P-450 Heme Proteins: Oxidoreductases Non-Heme Proteins: Iron-Sulfur Clusters Non-Heme Proteins: Mononuclear Iron Proteins Volume 2 IRON continued Non-Heme Proteins: Dinuclear Iron Proteins ...
Albrecht Messerschmidt +3 more
openaire +3 more sources
Volume 1 IRON Heme Proteins: Oxygen Storage and Oxygen Transport Proteins Heme Proteins: Cytochromes Heme Proteins: Cytochrome Peroxidases Heme Proteins: Cytochrome P-450 Heme Proteins: Oxidoreductases Non-Heme Proteins: Iron-Sulfur Clusters Non-Heme Proteins: Mononuclear Iron Proteins Volume 2 IRON continued Non-Heme Proteins: Dinuclear Iron Proteins ...
Albrecht Messerschmidt +3 more
openaire +3 more sources