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Stephen J. Lippard was born Oct. 12, 1940 in Pittsburgh, Pa. Stephen J. Lippard is the Arthur Amos Noyes Professor Emeritus of Chemistry at the Massachusetts Institute of Technology. His research spans the fields of biological and inorganic chemistry.
Lippard studies biological interactions involving metal ions, focusing on reactions and physical and structural properties of metal complexes. Such complexes can be useful as cancer drugs and as models for the active sites of metalloproteins. Metal ions also promote key biological reactions as signaling agents; metal complexes can be employed to sense biological signaling agents.
The Lippard group also determined the structure of the component proteins of methane monooxygenase (MMO), an enzyme from aerobic bacteria that converts methane (natural gas) and oxygen to liquid methanol and water in the first step of their life process. They elucidated several key steps in the activation of oxygen and methane, which takes place at a closely spaced pair of iron atoms in the enzyme. This chemistry is related to that used in bioremediation, processes by which microorganisms are employed to clean the environment. Examples include removal of trichloroethylene from drinking water and the cleanup of oil spills from the land. The structure of the hydroxylase component of MMO in complex with a small regulatory protein termed MMOB provided insight into the regulation of substrate access to the diiron active site. Oxygen and methane, but not electrons and protons, traverse a hydrophobic channel to the diiron center only when the reduced form of MMOH/MMOB is present, preventing unwanted quenching of diiron(III) peroxo and diiron(IV) oxo intermediates. After methanol and water formation, the channel is disrupted by protein side chain movements as the reductase comes in to form the reduced enzyme. Structures of the related hydroxylase enzymes from toluene/o-xylene monooxygenase and phenol hydroxylase, the latter in complex with its regulatory protein, were determined. Oxygenated intermediates in the catalytic cycles of the enzymes have been identified and studied in detail. Numerous synthetic carboxylate-bridged di- and polyiron complexes have been prepared and investigated in conjunction with this project, which has been successfully completed and is no longer a subject of active investigation.
Lippard studies biological interactions involving metal ions, focusing on reactions and physical and structural properties of metal complexes. Such complexes can be useful as cancer drugs and as models for the active sites of metalloproteins. Metal ions also promote key biological reactions as signaling agents; metal complexes can be employed to sense biological signaling agents.
The Lippard group also determined the structure of the component proteins of methane monooxygenase (MMO), an enzyme from aerobic bacteria that converts methane (natural gas) and oxygen to liquid methanol and water in the first step of their life process. They elucidated several key steps in the activation of oxygen and methane, which takes place at a closely spaced pair of iron atoms in the enzyme. This chemistry is related to that used in bioremediation, processes by which microorganisms are employed to clean the environment. Examples include removal of trichloroethylene from drinking water and the cleanup of oil spills from the land. The structure of the hydroxylase component of MMO in complex with a small regulatory protein termed MMOB provided insight into the regulation of substrate access to the diiron active site. Oxygen and methane, but not electrons and protons, traverse a hydrophobic channel to the diiron center only when the reduced form of MMOH/MMOB is present, preventing unwanted quenching of diiron(III) peroxo and diiron(IV) oxo intermediates. After methanol and water formation, the channel is disrupted by protein side chain movements as the reductase comes in to form the reduced enzyme. Structures of the related hydroxylase enzymes from toluene/o-xylene monooxygenase and phenol hydroxylase, the latter in complex with its regulatory protein, were determined. Oxygenated intermediates in the catalytic cycles of the enzymes have been identified and studied in detail. Numerous synthetic carboxylate-bridged di- and polyiron complexes have been prepared and investigated in conjunction with this project, which has been successfully completed and is no longer a subject of active investigation.
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Spherical Nucleic Acidspp.1585-1591, (2020)
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#Papers: 1235
#Citation: 111301
H-Index: 154
G-Index: 288
Sociability: 7
Diversity: 3
Activity: 15
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