Characterization of the membrane-bound succinic dehydrogenase of Micrococcus lysodeikticus.

Abstract:

:The occurrence of succinic dehydrogenase [succinic:(acceptor) oxidoreductase, EC 1.3.99.1] in membrane fractions of Micrococcus lysodeikticus was investigated. The enzyme could be purified 10-fold, by deoxycholate treatment. Butanol extraction of membranes yielded an active fraction, nonsedimentable at 130,000 x g for 2 hr and altered in its phospholipid content relative to membranes. The activity of the enzyme in particulate preparations was decreased in the presence of competitive inhibitors and by compounds known to react with iron, sulfhydryl groups, and flavine. In this respect, the bacterial succinic dehydrogenase is similar to the enzyme derived from yeast and mammalian sources. In certain membrane fractions, Ca(2+) and Mg(2+) exhibited inhibitory effects whereas Triton X-100 caused activation. The enzyme could also be activated by substrate. In the phenazine reductase assay, incomplete reduction of electron acceptor was observed upon addition of divalent cations and iron binding agents.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Pollock JJ,Linder R,Salton MR

doi

10.1128/JB.107.1.230-238.1971

subject

Has Abstract

pub_date

1971-07-01 00:00:00

pages

230-8

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

107

pub_type

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