Substrates but not inhibitors alter the redox potentials of monoamine oxidases

Antioxidants and Redox Signaling

Volumn 3, Issue 5, 2001, Pages 723-729

  Sablin, S O ^a   Ramsay, R R ^a  

^a UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

4,4' DITHIODIPYRIDINE; AMINE; FLAVINE ADENINE NUCLEOTIDE; MONOAMINE OXIDASE INHIBITOR; SEMIQUINONE;

ARTICLE; ELECTRON TRANSPORT; ENZYME INHIBITION; ENZYME SUBSTRATE; OXIDATION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; REDUCTION; THERMODYNAMICS;

GYMNOMYZA SAMOENSIS;

EID: 0035205469     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/15230860152664920     Document Type: Article

References (14)

1. A potentiometric study of the flavin semiquinone equilibrium
2. Kinetic studies on the mechanism of monoamine oxidase
3. A simple method for the determination of redox potentials
4. The kinetic mechanism of monoamine oxidase A
5. Stopped-flow studies on the mechanism of the oxidation of N-methyl-4-phenyltetrahydropyridine (MPTP) by bovine liver monoamine oxidase B
6. Redox properties of the flavin cofactor of monoamine oxidases A and B and their relationship to the kinetic mechanism
7. Monoamine oxidase contains a redox-active disulfide
8. Interaction of tetrahydrostilbazoles with monoamine oxidases A and B
9. Monoamine oxidase from beef liver mitochondria: Simplified isolation procedure, properties, and determination of its cysteinyl flavin content
10. Substrate-specific enhancement of the oxidative half-reaction of monoamine oxidase
11. Nonstereospecific reduction of monoamine oxidase from bovine liver by analogues of amphetamine
12. Biochemistry and genetics of monoamine oxidase
13. Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD