Scholars@Duke
Aristobulo Loaiza

Aristobulo Loaiza

Adjunct Instructor in the Engineering Graduate and Professional Programs
Engineering Graduate and Professional Programs
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Selected Publications

Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.

Journal Article European biophysics journal : EBJ · August 2011 Phenylalanine hydroxylase (PAH), a non-heme iron enzyme, is responsible for the phenylalanine conversion to tyrosine. Its malfunction causes phenylketonuria (PKU). To better understand how protein structure and folding profiles are affected by the metal co ... Full text Cite

Kinetics of thermal unfolding of phenylalanine hydroxylase variants containing different metal cofactors (FeII, CoII, and ZnII) and their isokinetic relationship.

Journal Article Inorganic chemistry · June 2008 The kinetics of thermal unfolding of apo- and holo-Chromobacterium violaceum phenylalanine hydroxylase (cPAH) was investigated using circular dichroism (CD) over the temperature range 44-76 degrees C. In addition to the native cofactor (FeII), the unfoldin ... Full text Cite

Effect of temperature, pH, and metals on the stability and activity of phenylalanine hydroxylase from Chromobacterium violaceum.

Journal Article Journal of inorganic biochemistry · March 2005 Phenylalanine hydroxylase (PAH) is a non-heme iron dioxygenase catalyzing the conversion of phenylalanine to tyrosine and is present in both prokaryotic and eukaryotic organisms. A relatively simple PAH is expressed by Chromobacterium violaceum, a gram-neg ... Full text Cite