Interaction of purified plant alternative oxidase from Arum maculatum with pyruvate

Moore, A, Affourtit, C and Carré, J (2011) Interaction of purified plant alternative oxidase from Arum maculatum with pyruvate. FEBS Letters, 585 (2). pp. 397-401. ISSN 0014-5793

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Abstract

Plant alternative oxidase (AOX) activity in isolated mitochondria is regulated by carboxylic acids, but reaction and regulatory mechanisms remain unclear. We show that activity of AOX protein purified from thermogenic Arum maculatum spadices is sensitive to pyruvate and glyoxylate but not succinate. Rapid, irreversible AOX inactivation occurs in the absence of pyruvate, whether or not duroquinol oxidation has been initiated, and is insensitive to duroquinone. Our data indicate that pyruvate stabilises an active conformation of AOX, increasing the population of active protein in a manner independent of reducing substrate and product, and are thus consistent with an exclusive effect of pyruvate on the enzymes apparent Vmax.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Anthony Moore
Date Deposited: 06 Feb 2012 19:19
Last Modified: 16 Jul 2012 12:08
URI: http://sro.sussex.ac.uk/id/eprint/20110
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