Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase.

Journal article

The final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylate (ACC) oxidase, a member of the non-heme iron(II) dependent family of oxygenases and oxidases, which has a requirement for ascorbate as a co-substrate and carbon dioxide as an activator. ACC oxidase (tomato) has a particularly short half-life under catalytic conditions undergoing metal-catalyzed oxidative (MCO) fragmentation. Sequence comparisons of ACC oxidases with is...

Expand abstract

Authors: Zhang, Z; Barlow, J; Baldwin, J; Schofield, C

• Publication status: Published
• Journal: Biochemistry
• Volume: 36
• Issue: 50
• Pages: 15999-16007
• Publication date: 1997-12-01
• DOI: 10.1021/bi971823c
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Amino Acid Sequence; Sequence Alignment; Ferrous Compounds; Amino Acids, Cyclic; Oxidation-Reduction; Mutagenesis, Site-Directed; Molecular Sequence Data; Protein Conformation; Protein Folding; Amino Acids; Catalysis; Electrophoresis, Polyacrylamide Gel; Sequence Analysis; Conserved Sequence; Lycopersicon esculentum; Binding Sites; Sequence Homology, Amino Acid; Nonheme Iron Proteins; Ethylenes; Amino Acid Oxidoreductases; Reactive Oxygen Species