Jack Peisach, Ph.D.

Professor
Office: FOR G18N
Tel: 718-430-2175
Email: peisach@aecom.yu.edu

Transition metals in biological systems play an important role in oxygen binding, transport, and activation, in electron transfer, and in enzyme catalysis. Research in this laboratory is directed towards understanding the structure and function of metal binding sites in the aforementioned processes, largely through spectroscopic analysis. The tools available include optical, continuous wave, and pulsed EPR spectroscopy. Students wishing to pursue a degree in this laboratory can elect topics related to 1) the mechanisms of oxygen activation in drug-DNA cleavage reactions and in hemoprotein catalysis; 2) the role of protein structure in modulating catalytic activity and ligand stabilization through hydrogen bonding at metal sites; 3) mapping out active site structures with paramagnetic probes; the mode of substrate binding in metallo enzymes; 4) making distance measurements between bound substrates and metal ions coordinated to biomolecules and between paramagnetic centers; and 5) the determination of nuclear quadrupole, nuclear hyperfine and g tensor orientations at metal centers.

These approaches are being applied to iron bleomycin catalyzed cleavage of DNA, copper- iron-, cobalt- and mangano proteins, as well as their various mutant and metal substituted forms, including phenylalanine hydroxylase, myoglobin, hemoglobin, pyruvate kinase, superoxide dismutase, stellacyanin, and azurin, in addition to low molecular weight model compounds of known structure.
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