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Site-directed mutagenesis as a probe to study the mechanism of sheep liver 6-phosphogluconate dehydrogenase.
(2006)
All mutant enzymes in the 2'-phosphate site exhibit an increase in KNADP that ranges from 6-fold to 80-fold. A 7-fold increase in the primary kinetic 13C-isotope effect minus 1 in all mutant enzymes indicates that the ...
The structure and function of YPD1, a histidine-containing phosphotransfer protein from yeast.
(2001)
Finally, through molecular modeling and structural comparisons, a general model of how YPD1 and response regulator domains might interact was proposed. It seems likely that YPD1 binds to response regulator domains through ...
Identification and analysis of the response regulator binding site on the surface of the histidine-containing phosphotransfer protein YPD1 from Saccharomyces cerevisiae.
(2003)
The results from the yeast two-hybrid screens were confirmed by the X-ray crystal structure of the SLN1-R1/YPD1 complex. This structure is the first to reveal protein-protein interactions between a monomeric HPt domain and ...
Iron uptake in Gram-negative and Gram-positive bacteria.
(2006)
Bacteria, including both Gram-positive and Gram-negative bacteria, utilize iron sources from the environment. Iron uptake systems in Gram-negative bacteria are well studied. Escherichia coli FepA transports certain catecholate ...
Binding and transport through ferric siderophore receptors, FepA and FhuA.
(2006)
Under iron deficient conditions, Gram-negative bacteria like E. coli secrete siderophores to chelate iron in the extracellular medium. Ligand-gated porins (LGPs) transport the ferric siderophore complexes across the outer ...
A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin.
(2007)
This dissertation deals with the interaction of the biologically important nitrogen oxides (nitric oxide and nitrite) with manganese and ruthenium centers in small inorganic porphyrin and nonporphyrin complexes as well as ...