Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase. 1980

M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan

UI MeSH Term Description Entries
D007506 Iron-Sulfur Proteins A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation. Iron-Sulfur Protein,Iron Sulfur Proteins,Iron Sulfur Protein,Protein, Iron-Sulfur,Proteins, Iron Sulfur,Proteins, Iron-Sulfur,Sulfur Proteins, Iron
D007658 Ketone Oxidoreductases Oxidoreductases that are specific for KETONES. Oxidoreductases, Ketone
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008667 Metalloproteins Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) Metalloprotein
D008982 Molybdenum A metallic element with the atomic symbol Mo, atomic number 42, and atomic weight 95.95. It is an essential trace element, being a component of the enzymes xanthine oxidase, aldehyde oxidase, and nitrate reductase. Molybdenum-98,Molybdenum 98
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D004578 Electron Spin Resonance Spectroscopy A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING. ENDOR,Electron Nuclear Double Resonance,Electron Paramagnetic Resonance,Paramagnetic Resonance,Electron Spin Resonance,Paramagnetic Resonance, Electron,Resonance, Electron Paramagnetic,Resonance, Electron Spin,Resonance, Paramagnetic
D005420 Flavoproteins Flavoprotein
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations

Related Publications

M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
March 1982, Biochemistry,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
November 1979, The Journal of biological chemistry,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
September 1983, The Journal of biological chemistry,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
August 1976, The Biochemical journal,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
February 1974, Biochemical and biophysical research communications,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
May 1985, Biochemistry,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
July 1973, Biochemical and biophysical research communications,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
October 1982, The Journal of biological chemistry,
M J Barber, and M P Coughlan, and M Kanda, and K V Rajagopalan
February 1980, The Biochemical journal,
Copied contents to your clipboard!