l ‐Lactate generates hydrogen peroxide in purified rat liver mitochondria due to the putative  l ‐lactate oxidase localized in the intermembrane space | Zendy

de Bari Lidia | Zendy; Valenti Daniela | Zendy; Atlante Anna | Zendy; Passarella Salvatore | Zendy

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l ‐Lactate generates hydrogen peroxide in purified rat liver mitochondria due to the putative l ‐lactate oxidase localized in the intermembrane space

Author(s) -

de Bari Lidia,

Valenti Daniela,

Atlante Anna,

Passarella Salvatore

Publication year - 2010

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2010.03.038

Subject(s) - intermembrane space , biochemistry , submitochondrial particle , hydrogen peroxide , lactate dehydrogenase , respiratory chain , peroxisome , oxidase test , chemistry , nad+ kinase , mitochondrion , cytosol , oxygen , mitochondrial matrix , mitochondrial intermembrane space , enzyme , organic chemistry , bacterial outer membrane , escherichia coli , gene

In order to ascertain whether and how mitochondria can produce hydrogen peroxide (H 2 O 2 ) as a result of l ‐lactate addition, we monitored H 2 O 2 generation in rat liver mitochondria and in submitochondrial fractions free of peroxisomal and cytosolic contamination. We found that H 2 O 2 is produced independently on the respiratory chain with 1:1 stoichiometry with pyruvate, due to a putative flavine‐dependent l ‐lactate oxidase restricted to the intermembrane space. The l ‐lactate oxidase reaction shows a hyperbolic dependence on l ‐lactate concentration and is inhibited by NAD + in a competitive manner, being the enzyme different from the l ‐lactate dehydrogenase isoenzymes as shown by their pH profiles.

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