Molecular properties of succinate dehydrogenase isolated from Micrococcus luteus (lysodeikticus).

Abstract:

:Succinate dehydrogenase (EC 1.3.99.1) of Micrococcus luteus was selectively precipitated from Triton X-100-solubilized membranes by using specific antiserum. The precipitated enzyme contained equimolar amounts of four polypeptides with apparent molecular weights of 72,000, 30,000, 17,000, and 15,000. The 72,000 polypeptide possessed a covalently bound flavin prosthetic group and appeared to be strongly antigenic as judged by immunoprinting experiments. Low-temperature absorption spectroscopy revealed the presence of cytochrome b556 in the antigen complex. By analogy with succinate dehydrogenase purified from other sources, the 72,000 and 30,000 polypeptides were considered to represent subunits of the succinate dehydrogenase enzyme, whereas one (or both) of the low-molecular-weight polypeptides was attributed to the apoprotein of the b-type cytochrome. A succinate dehydrogenase antigen cross-reacting with the M. luteus enzyme complex could be demonstrated in membranes of Micrococcus roseus, Micrococcus flavus, and Sarcina lutea, but not in the membranes isolated from a wide variety of other gram-positive and gram-negative bacteria.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Crowe BA,Owen P

doi

10.1128/JB.153.3.1493-1501.1983

subject

Has Abstract

pub_date

1983-03-01 00:00:00

pages

1493-501

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

153

pub_type

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