Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas.

Autor: Guan HH; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Hsieh YC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Lin PJ; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan.; Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30043, Taiwan., Huang YC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Yoshimura M; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Chen LY; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan.; Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, 701, Taiwan., Chen SK; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan.; Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, 701, Taiwan., Chuankhayan P; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Lin CC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Chen NC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan., Nakagawa A; Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan., Chan SI; Institute of Chemistry, Academia Sinica, Nankang, Taipei, 11529, Taiwan.; Noyes Laboratory 127-72, California Institute of Technology, Pasadena, CA, 91125, USA., Chen CJ; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan. cjchen@nsrrc.org.tw.; Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, 701, Taiwan. cjchen@nsrrc.org.tw.; Department of Physics, National Tsing Hua University, Hsinchu, 30043, Taiwan. cjchen@nsrrc.org.tw.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2018 Oct 08; Vol. 8 (1), pp. 14935. Date of Electronic Publication: 2018 Oct 08.
DOI: 10.1038/s41598-018-33193-5
Abstrakt: The membrane-embedded quinol:fumarate reductase (QFR) in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain. The electron/proton-transfer pathways in QFRs remain controversial. Here we report the crystal structure of QFR from the anaerobic sulphate-reducing bacterium Desulfovibrio gigas (D. gigas) at 3.6 Å resolution. The structure of the D. gigas QFR is a homo-dimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme b L in the hydrophobic subunit C. This location of the menaquinone-binding site differs from the menaquinol-binding cavity proposed previously for QFR from Wolinella succinogenes. The observed bound menaquinone might serve as an additional redox cofactor to mediate the proton-coupled electron transport across the membrane. Armed with these structural insights, we propose electron/proton-transfer pathways in the quinol reduction of fumarate to succinate in the D. gigas QFR.
Databáze: MEDLINE
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