- Bachelor of Arts, Harvard University, 1963
- Doctor of Philosophy, Johns Hopkins University, 1967
Chemical and spectroscopic properties of the heme sites in animal and plant hemoglobins.
My principal research interest is in characterizing the abilities of hemoglobin, myoglobin, and soybean leghemoglobin (all proteins with known physiological roles that involve reversible O2 binding) to catalyze the reactions of O2 with the biological reducing agents NADH and NADPH to produce hydrogen peroxide, as well as to catalyze the reaction of hydrogen peroxide with NADH and NADPH to produce water. At certain pH’s the two reactions can be teased apart, and at other pH’s they combine and the hydrogen peroxide does not accumulate. My experimental studies on the stoichiometry of these reactions have run afoul of the problem of trying to use spectrophotometric methods to measure hydrogen peroxide concentrations in the presence of NADH and NADPH. Therefore, I am examining several different spectrophotometric methods for assaying hydrogen peroxide in order to establish which they are partly or completely inhibited by NADH and NADPH, and whether either of two strategies (removal of NADH through oxidation by enzyme-catalyzed reactions, or three-dimensional calibration curves that take into account concentrations of NADH and NADPH) will circumvent the inhibition. The information gained will allow more accurate determination of the ratio of NADH (or NADPH) consumed to hydrogen peroxide produced or consumed in these reactions.
I also have scholarly interests in clarifying some misapprehensions I have encountered in textbooks and the research literature: overly simplistic interpretations of patterns of inhibition and cooperativity in enzyme kinetics, mechanistic over-interpretation of saturation kinetics, and the meaning of reducing sugars. My clarification efforts involve simple derivations and some experimental work.
Bioorganic Chem, General Chem, Origins of Cancer
- W.H. Fuchsman, "Plant Hemoglobins", Adv. Comp. Env. Physiol., 1992, 13, 23.