ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Evidence for H2O2 as the product of reduction of oxygen by alternative oxidase in mitochondria from potato tubers

Bhate, Radha H and Ramasarma, T (2009) Evidence for H2O2 as the product of reduction of oxygen by alternative oxidase in mitochondria from potato tubers. In: Archives of biochemistry and biophysics, 486 (2). pp. 165-169.

[img] PDF
3full_text.pdf - Published Version
Restricted to Registered users only

Download (369kB) | Request a copy
Official URL: http://www.sciencedirect.com/science?_ob=ArticleUR...


Oxygen Consumption by alternative oxidase (AOX), present in mitochondria of many angiosperms, is known to be cyanide-resistant in contrast to cytochrome oxidase. Its activity in potato tuber (Solarium tuberosum L.) was induced following chilling treatment at 4 degrees C.About half of the total O-2 consumption of succinate oxidation in such mitochondria was found to be sensitive to SHAM, a known inhibitor of AOX activity. Addition of catalase to the reaction mixture of AOX during the reaction decreased the rate of SHAM-sensitive oxygen consumption by nearly half, and addition at the end of the reaction released nearly half of the consumed oxygen by AOX, both typical of catalase action on H2O2. These findings with catalase suggest that the product of reduction of AOX is H2O2 and not H2O, as previously Surmised. In potatoes Subjected to chill stress (4 degrees C) for periods of 3, 5 and >= 8 days the activity of AOX in mitochondria increased progressively with a corresponding increase in the AOX protein detected by immunoblot of the protein.

Item Type: Journal Article
Publication: Archives of biochemistry and biophysics
Publisher: Elsevier science
Additional Information: Copyright for this article belongs to Elsevier science.
Keywords: Alternative oxidase; Potato mitochondria; Chilling enhances AOX ;activity; H2O2-product of consumed O-2; Inhibition by SHAM;Catalase-dependent O-2 release.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 17 Jul 2009 10:21
Last Modified: 11 Oct 2018 14:29
URI: http://eprints.iisc.ac.in/id/eprint/21144

Actions (login required)

View Item View Item