Electron paramagnetic resonance studies of succinate:ubiquinone oxidoreductase from Paracoccus denitrificans : Evidence for a magnetic interaction between the 3Fe-4S cluster and cytochrome b

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Waldeck, A. ReginaldCalifornia Institute of Technology (author)

Electron paramagnetic resonance studies of succinate:ubiquinone oxidoreductase from Paracoccus denitrificans : Evidence for a magnetic interaction between the 3Fe-4S cluster and cytochrome b

Article/chapterEnglish1997

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Elsevier BV,1997

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LIBRIS-ID:oai:lup.lub.lu.se:634429c2-bb9c-4cc5-8734-4e68d16088aa
https://lup.lub.lu.se/record/634429c2-bb9c-4cc5-8734-4e68d16088aaURI
https://doi.org/10.1074/jbc.272.31.19373DOI

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Language:English
Summary in:English

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Electron paramagnetic resonance (EPR) studies of succinate:ubiquinone oxidoreductase (SQR) from Paracoccus denitrificans have been undertaken in the purified and membrane-bound states, Spectroscopic ''signatures'' accounting for the three iron-sulfur clusters (2Fe-2S, 3Fe-4S, and 4Fe-4S), cytochrome b, flavin, and protein-bound ubisemiquinone radicals have been obtained in air-oxidized, succinate-reduced, and dithionite-reduced preparations at 4-10 K. Spectra obtained at 170 K in the presence of excess succinate showed a signal typical of that of a flavin radical, but superimposed with another signal. The superimposed signal originated from two bound ubisemiquinones, as shown by spectral simulations, Power saturation measurements performed on the air-oxidized enzyme provided evidence for a weak magnetic dipolar interaction operating between the oxidized 3Fe-4S cluster and the oxidized cytochrome b. Power saturation experiments performed on the succinate- and dithionite-reduced forms of the enzyme demonstrated that the 4Fe-4S cluster is coupled weakly to both the 2Fe-2S and the 3Fe-4S clusters, Quantitative interpretation of these power saturation experiments has been achieved through redox calculations. They revealed that a spin-spin interaction between the reduced 3Fe-4S cluster and the cytochrome b (oxidized) may also exist. These findings form the first direct EPR evidence for a close proximity (less than or equal to 2 nm) of the high potential 3Fe-4S cluster, situated in the succinate dehydrogenase part of the enzyme, and the low potential, low spin b-heme in the membrane anchor of the enzyme.

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NATURVETENSKAP Biologi Mikrobiologi hsv//swe
NATURAL SCIENCES Biological Sciences Microbiology hsv//eng

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Stowell, Michael H. B.California Institute of Technology (author)
Lee, Hung KayCalifornia Institute of Technology (author)
Hung, Shao-ChingCalifornia Institute of Technology (author)
Matsson, Mikael (author)
Hederstedt, LarsLund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science(Swepub:lu)mikb-lhe (author)
Ackrell, Brian A.C.University of California, San Francisco (author)
Chan, Sunney I.California Institute of Technology (author)
California Institute of TechnologyMolekylär cellbiologi (creator_code:org_t)

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In:Journal of Biological Chemistry: Elsevier BV1083-351X0021-9258

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NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Microbiology

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By the university: Lund University

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