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The prosthetic groups of succinate dehydrogenase: 30 years from discovery to identification
Author(s) -
Singer Thomas P.,
Johnson Michael K.
Publication year - 1985
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 - 10.1016/0014-5793(85)81282-5
Subject(s) - succinate dehydrogenase , flavin group , electron paramagnetic resonance , enzyme , chemistry , dehydrogenase , fumarate reductase , electron transfer , crystallography , stereochemistry , biochemistry , nuclear magnetic resonance , organic chemistry , physics
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.