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Succinate oxidase in Neurospora.

D J West, D O Woodward

Journal of Bacteriology

|February 1, 1973

Summary

Neurospora crassa mitochondria possess two succinate oxidase states with differing affinities for succinate. Adenosine triphosphate (ATP) and Mg(2+) stabilize the high K(m) state, influencing enzyme kinetics.

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Area of Science:

Biochemistry
Mitochondrial Respiration
Enzyme Kinetics

Background:

Succinate oxidase is a key enzyme in mitochondrial respiration.
Understanding its kinetic properties is crucial for elucidating cellular energy production.

Purpose of the Study:

To identify and characterize distinct kinetic states of succinate oxidase in Neurospora crassa mitochondria.
To investigate factors influencing the stability and activity of these states.

Main Methods:

Enzyme kinetic assays using isolated mitochondria from Neurospora crassa.
Determination of Michaelis constant (K(m)) for succinate.
Analysis of enzyme activity across a pH range.
Inhibition studies with fumarate and malonate.
Investigation of stabilization effects by adenosine triphosphate (ATP) and Mg(2+).

Main Results:

Two kinetically distinct states of succinate oxidase were identified with high (4.1 x 10(-3)m) and low (3.5 x 10(-4)m) K(m) values for succinate.
The high K(m) state was observed in freshly isolated mitochondria and stabilized by ATP plus Mg(2+).
The low K(m) state emerged upon in vitro deterioration of mitochondria from younger mycelia and exhibited nonclassical inhibition patterns.

Conclusions:

Neurospora crassa mitochondria exhibit at least two kinetic forms of succinate oxidase.
Mitochondrial age and intracellular energy status (ATP levels) likely influence the predominant succinate oxidase state.
ATP and Mg(2+) play a role in maintaining the high K(m) state, suggesting regulatory mechanisms linked to cellular energy demand.

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