Work

Succinate Dehydrogenase

Year: 1982

Type: article

Abstract: A procedure was developed for the partial purification of succinate dehydrogenase from mung bean (Vigna radiata L.) hypocotyls and soybean (Glycine max [L] Merr. v. Ransom) cotyledons. The procedure utilized a Triton X-100 extraction followed by ammonium sulfate precipitation. The final fraction was enriched in two polypeptides with approximate molecular weights of 67,000 and 30,000 daltons, exhibited a pH optima of 7.0 to 7.5, contained a b-type cytochrome, and exhibited the characteristic ferredoxin-type and high potential iron-sulfur protein-type electron paramagnetic resonance signals reported for the iron-sulfur centers of mammalian succinate dehydrogenase. Inhibition constants of 1.15 and 24.6 micromolar for oxaloacetate and malonate, respectively, were obtained.

Source: PLANT PHYSIOLOGY

DOI: 10.1104/pp.70.6.1577

Authors: John J. Burke, James N. Siedow, Donald E. Moreland

Institutions: Agricultural Research Service, United States Department of Agriculture, North Carolina State University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,851

Funders: U.S. Department of Agriculture, U.S. Public Health Service, National Institute of General Medical Sciences