Probing structure-function relations in heme-containing oxygenases and peroxidases.

J H Dawson

doi:10.1126/science.3358128

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PubMed · 3358128

Probing structure-function relations in heme-containing oxygenases and peroxidases.

J H Dawson

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Abstract

Structural factors that influence functional properties are examined in the case of four heme enzymes: cytochrome P-450, chloroperoxidase, horseradish peroxidase, and secondary amine mono-oxygenase. The identity of the axial ligand, the nature of the heme environment, and the steric accessibility of the heme iron and heme edge combine to play major roles in determining the reactivity of each enzyme. The importance of synthetic porphyrin models in understanding the properties of the protein-free metal center is emphasized. The conclusions described herein have been derived from studies at the interface between biological and inorganic chemistry.

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Catalysis Chloride Peroxidase Cytochrome P-450 Enzyme System Hemeproteins Horseradish Peroxidase Oxygenases Peroxidases Structure-Activity Relationship Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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J H Dawson. 1988-04-22. Probing structure-function relations in heme-containing oxygenases and peroxidases.. https://doi.org/10.1126/science.3358128

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