Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Stephen F. Gheller"'
Autor:
Louis M. Rendina, David C. R. Hockless, Meta Sterns, Stephen F. Gheller, Graham A. Heath, Rowena L. Paul
Publikováno v:
Journal of the Chemical Society, Dalton Transactions. :4143-4146
Orange platelets of [Pt(tmtaa)], where H2tmtaa = 6,8,15,17-tetramethyl-5,6,9,14,15,18-hexahydrodibenzo[b,i][l,4,8,11]tetraazacyclotetradecine, show the expected ‘pseudo-planar’ centrosymmetric macrocyclic conformation but red needles of another [
Publikováno v:
Journal of the American Chemical Society. 115:2714-2722
A new oxo transfer reaction system of relevance to the molybdenum oxotransferase group of enzymes has been developcd. A set of ligands and their sterically hindered Mo VI O 2 complexes have been prepared.
Publikováno v:
ChemInform. 23
Autor:
David C. R. Hockless, Graham A. Heath, John E. McGrady, David G. Humphrey, Stephen F. Gheller
Publikováno v:
ChemInform. 26
Publikováno v:
Inorganica Chimica Acta. 170:115-122
Electrochemical examination of the iron-molybdenum cofactor (FeMoco) extracted from the MoFe protein of Azotobacter vinelandii nitrogenase reveals that this important biological cluster exists in a variety of chemical forms whose numbers, proportions
Autor:
Stephen F. Gheller, Glen F. Bailey, Franklin A. Schultz, William E. Newton, Benjamin J. Feldman
Publikováno v:
Analytical Biochemistry. 185:170-175
Cell designs, experimental protocols, and results for electrochemical investigation of small quantities of biological materials under anaerobic conditions are reported. Three types of electrochemical experiments are considered: (i) cyclic voltammetry
Publikováno v:
Journal of the American Chemical Society. 114:6934-6935
Autor:
Stephen F. Gheller, B.J. Feldman, William E. Newton, P. Frank, Keith O. Hodgson, Britt Hedman, Franklin A. Schultz
Publikováno v:
Journal of Inorganic Biochemistry. 43:479
Publikováno v:
Biochemical and Biophysical Research Communications. 152:629-635
The number of electrons involved in the more positive of the two redox couples of the iron-molybdenum cofactor of Azotobacter vinelandii nitrogenase has been investigated by controlled potential coulometry in both the oxidizing and reducing direction