TY - CHAP
T1 - Flavoprotein Disulfide Reductases
T2 - Advances in Chemistry and Function
AU - Argyrou, Argyrides
AU - Blanchard, John S.
N1 - Funding Information:
We thank Dr. Matthew W. Vetting for preparing Figs. 2A, 2B, and 14A . The work was supported by NIH grant GM33449.
PY - 2004
Y1 - 2004
N2 - The flavoprotein disulfide reductases represent a family of enzymes that show high sequence and structural homology. They catalyze the pyridine-nucleotide-dependent reduction of a variety of substrates, including disulfide-bonded substrates (lipoamide dehydrogenase, glutathione reductase and functional homologues, thioredoxin reductase, and alkylhydroperoxide reductase), mercuric ion (mercuric ion reductase), hydrogen peroxide (NADH peroxidase), molecular oxygen (NADH oxidase), and the reductive cleavage of a carbonyl-activated carbon-sulfur bond followed by carboxylation (2-ketopropyl-coenzyme-M carboxylase{plus 45 degree rule}oxidoreductase). They use at least one nonflavin redox center to transfer electrons from reduced pyridine nucleotide to their substrate through flavin adenine dinucleotide. The nature of the nonflavin redox center located adjacent to the flavin varies and three types have been identified: an enzymic disulfide (most commonly), an enzymic cysteine sulfenic acid (NADH peroxidase and NADH oxidase), and a mixed Cys-S-S-CoA disulfide (coenzyme A disulfide reductase). Selection of the particular nonflavin redox center and utilization of a second, or even a third, nonflavin redox center in some cases presumably represents the most efficient strategy for reduction of the individual substrate.
AB - The flavoprotein disulfide reductases represent a family of enzymes that show high sequence and structural homology. They catalyze the pyridine-nucleotide-dependent reduction of a variety of substrates, including disulfide-bonded substrates (lipoamide dehydrogenase, glutathione reductase and functional homologues, thioredoxin reductase, and alkylhydroperoxide reductase), mercuric ion (mercuric ion reductase), hydrogen peroxide (NADH peroxidase), molecular oxygen (NADH oxidase), and the reductive cleavage of a carbonyl-activated carbon-sulfur bond followed by carboxylation (2-ketopropyl-coenzyme-M carboxylase{plus 45 degree rule}oxidoreductase). They use at least one nonflavin redox center to transfer electrons from reduced pyridine nucleotide to their substrate through flavin adenine dinucleotide. The nature of the nonflavin redox center located adjacent to the flavin varies and three types have been identified: an enzymic disulfide (most commonly), an enzymic cysteine sulfenic acid (NADH peroxidase and NADH oxidase), and a mixed Cys-S-S-CoA disulfide (coenzyme A disulfide reductase). Selection of the particular nonflavin redox center and utilization of a second, or even a third, nonflavin redox center in some cases presumably represents the most efficient strategy for reduction of the individual substrate.
UR - http://www.scopus.com/inward/record.url?scp=10644295071&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=10644295071&partnerID=8YFLogxK
U2 - 10.1016/S0079-6603(04)78003-4
DO - 10.1016/S0079-6603(04)78003-4
M3 - Chapter
C2 - 15210329
AN - SCOPUS:10644295071
SN - 0125400780
SN - 9780125400787
T3 - Progress in Nucleic Acid Research and Molecular Biology
SP - 89
EP - 142
BT - Progress in Nucleic Acid Research and Molecular Biology
PB - Academic Press Inc.
ER -