Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced 
Ferredoxin:NADP Oxidoreductase Structure

Demmer, Julius K.; Huang, Haiyan; Wang, Shuning; Demmer, Ulrike; Thauer, Rudolf K.; Ermler, Ulrich

doi:10.1074/jbc.M115.656520

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Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure

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Demmer, Julius K.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Huang, Haiyan
Max-Planck-Institute for Terrestrial Microbiology, Max Planck Society;

Wang, Shuning
Max-Planck-Institute for Terrestrial Microbiology, Max Planck Society;

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Demmer, Ulrike
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Thauer, Rudolf K.
Max-Planck-Institute for Terrestrial Microbiology, Max Planck Society;

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Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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引用

Demmer, J. K., Huang, H., Wang, S., Demmer, U., Thauer, R. K., & Ermler, U. (2015). Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure. The Journal of Biological Chemistry, 290(36), 21985-21885. doi:10.1074/jbc.M115.656520.

引用: https://hdl.handle.net/11858/00-001M-0000-002A-411C-C

要旨

NADH-dependent reduced ferredoxin:NADP oxidoreductase (NfnAB) is found in the cytoplasm of various anaerobic bacteria and archaea. The enzyme reversibly catalyzes the endergonic reduction of ferredoxin with NADPH driven by the exergonic transhydrogenation from NADPH onto NAD⁺. Coupling is most probably accomplished via the mechanism of flavin-based electron bifurcation. To understand this process on a structural basis, we heterologously produced the NfnAB complex of Thermotoga maritima in Escherichia coli, provided kinetic evidence for its bifurcating behavior, and determined its x-ray structure in the absence and presence of NADH. The structure of NfnAB reveals an electron transfer route including the FAD (a-FAD), the [2Fe-2S] cluster of NfnA and the FAD (b-FAD), and the two [4Fe-4S] clusters of NfnB. Ferredoxin is presumably docked onto NfnB close to the [4Fe-4S] cluster distal to b-FAD. NAD(H) binds to a-FAD and NADP(H) consequently to b-FAD, which is positioned in the center of the NfnAB complex and the site of electron bifurcation. Arg¹⁸⁷ is hydrogen-bonded to N₅ and O₄ of the bifurcating b-FAD and might play a key role in adjusting a low redox potential of the FADH^ˑ/FAD pair required for ferredoxin reduction. A mechanism of FAD-coupled electron bifurcation by NfnAB is proposed.