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Literature DB >> 7103946

Evidence that the activation of aconitase involves a conformation change.

Abstract

Reduction of the iron-sulphur cluster of aconitase initiates a slow increase in catalytic activity. It has been proposed that activation involves a conformational change in the protein. Direct evidence for this is presented here in the demonstration that, after reduction of the cluster, the progressive increase in activity is parallelled by an increase in the fluorescence of the protein.

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Year: 1982 PMID： 7103946 PMCID： PMC1158227 DOI： 10.1042/bj2030327

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

8 in total

1. The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase.

Authors: F J Ruzicka; H Beinert
Journal: J Biol Chem Date: 1978-04-25 Impact factor: 5.157

2. The mechanism of aconitase action. I. Preparation, physical properties of the enzyme, and activation by iron (II).

Authors: J J Villafranca; A S Mildvan
Journal: J Biol Chem Date: 1971-02-10 Impact factor: 5.157

Review 3. Fluorescence spectroscopic investigations of the dynamic properties of proteins, membranes and nucleic acids.

Authors: J R Lakowicz
Journal: J Biochem Biophys Methods Date: 1980 Jan-Feb

4. On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments.

Authors: M H Emptage; T A Kent; B H Huynh; J Rawlings; W H Orme-Johnson; E Münck
Journal: J Biol Chem Date: 1980-03-10 Impact factor: 5.157

2 in total

1. The relationship between the optical properties and the kinetic behaviour of ascorbate-inhibited alkaline phosphatase.

Authors: G E Martorana; E Meucci; A Ursitti; G A Miggiano; A Mordente; A Castelli
Journal: Biochem J Date: 1986-12-15 Impact factor: 3.857

2. Molecular forms of aconitase and their interconversions.

Authors: R R Ramsay; T P Singer
Journal: Biochem J Date: 1984-07-15 Impact factor: 3.857

2 in total

Evidence that the activation of aconitase involves a conformation change.

1. The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase.

2. The mechanism of aconitase action. I. Preparation, physical properties of the enzyme, and activation by iron (II).

Review 3. Fluorescence spectroscopic investigations of the dynamic properties of proteins, membranes and nucleic acids.

4. On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments.

5. Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.

6. The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster.

7. Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding.

8. Iron and aconitase activity.

1. The relationship between the optical properties and the kinetic behaviour of ascorbate-inhibited alkaline phosphatase.

2. Molecular forms of aconitase and their interconversions.