Probing Structure-Function Relations in Heme-Containing Oxygenases and Peroxidases

• Published in: Science (American Association for the Advancement of Science) Vol. 240; no. 4851; pp. 433 - 439
• Main Author: Dawson, John H.
• Format: Journal Article
• Language: English
• Published: Washington, DC The American Association for the Advancement of Science 22.04.1988; American Association for the Advancement of Science
• Subjects: Amines; Analysis; Analytical, structural and metabolic biochemistry; Atoms; Biochemistry; Biological and medical sciences; Biological markers; Catalysis; Chemistry; Chemistry, Physical and theoretical; Chloride Peroxidase; Cytochrome P-450; Cytochrome P-450 Enzyme System; Cytochromes; Enzymes; Enzymes and enzyme inhibitors; Frontiers in Chemistry; Fundamental and applied biological sciences. Psychology; Heme; Hemeproteins; Horseradish Peroxidase; Ligands; Molecular structure; Oxidoreductases; Oxygen; oxygenase; Oxygenases; peroxidase; Peroxidases; Peroxides; Physical chemistry; Porphyrins; Structure-Activity Relationship; Oxygenase; Hemoprotein; Structure activity relation; Enzyme; Oxidoreductase; Cytochrome P450; Heme; Peroxidase
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.3358128

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.