The prosthetic groups of succinate dehydrogenase: 30 years from discovery to identification

FEBS Letters

Johnson, Michael K.¹  Singer, Thomas P.¹ 

[1] Departments of Biochemistry-Biophysics and Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA

关键词: Channel;    Antagonist;    Agonist;    Dye anion radical;    Photoreduction;    Electron donor;    Electron acceptor;   

DOI  :  10.1016/0014-5793(85)81282-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recent studies using magnetic circular dichroism at cryogenic temperatures, electron paramagnetic resonance (EPR) and linear electric field effect-EPR (LEFE) of succinate dehydrogenase in membranes and in soluble, homogeneous preparations demonstrated the presence of 3 different Fe-S clusters in the mammalian enzyme, as well as in a similar bacterial enzyme, fumarate reductase from Escherichia coli. There is one each of the 2Fe, 3Fe, and 4Fe clusters. Thus, succinate dehydrogenase is the first enzyme which has been shown to contain all 3 of these Fe-S clusters. The enzyme also contains 1 mol 8α-[N(3)-histidyl]-FAD. It has taken the combined expertise of many laboratories and 15 years of effort to identify the flavin component, and nearly 3 decades to identify the Fe-S clusters. The data from physical methods appear to be internally consistent, in harmony with the results of chemical analysis, and provide a rational explanation for earlier results by the cluster extrusion method. There remains, however, a number of interesting and substantive questions for future investigations. This review traces the tortuous path, the many pitfalls and false leads, which have led us from the discovery of nonheme iron and ‘bound’ flavin in the enzyme to elucidation of their structures.

【 授权许可】

Unknown