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Flavoprotein disulfide reductases: advances in chemistry and function
Argyrides Argyrou1, John S Blanchard
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Progress in Nucleic Acid Research and Molecular Biology
|June 24, 2004
Summary
Flavoprotein disulfide reductases are enzymes that use a flavin adenine dinucleotide cofactor and non-flavin redox centers to reduce various substrates. Their diverse non-flavin centers enable efficient substrate-specific reduction strategies.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Flavoprotein disulfide reductases form a homologous enzyme family.
- These enzymes catalyze pyridine-nucleotide-dependent reductions.
Purpose of the Study:
- To detail the diverse substrates and redox mechanisms of flavoprotein disulfide reductases.
- To identify and categorize the non-flavin redox centers utilized by these enzymes.
Main Methods:
- Comparative analysis of enzyme sequences and structures.
- Substrate and cofactor interaction studies.
- Characterization of non-flavin redox centers.
Main Results:
- Identified a wide range of substrates including disulfide bonds, metal ions, and peroxides.
- Characterized three types of non-flavin redox centers: enzymic disulfide, cysteine sulfenic acid, and mixed Cys-S-S-CoA disulfide.
- Demonstrated electron transfer from pyridine nucleotides via flavin adenine dinucleotide to substrates.
Conclusions:
- The enzyme family exhibits significant sequence and structural homology.
- Non-flavin redox center diversity facilitates substrate-specific reduction efficiency.
- Enzyme strategy involves at least one, and sometimes multiple, non-flavin redox centers.