Identification of the coupling step in Na+-translocating NADH:quinone oxidoreductase from real-time kinetics of electron transfer
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- 作者：Nikolai P. Belevicha ; Yulia V. Bertsovab ; Marina L. Verkhovskayaa ; Alexander A. Baykovb ; Alexander V. Bogachevb ; bogachev@belozersky.msu.ru" class="auth_mail" title="E-mail the corresponding author
- 关键词：Cys4[Fe] ; a Fe ion coordinated by four cysteine residues ; FlH&minus ; ; anionic form of reduced flavin ; FlH ; neutral flavosemiquinone radical ; Fl&minus ; ; flavosemiquinone anion radical ; FMNB and FMNC ; FMN residues covalently bound to subunits NqrB and NqrC ; respectively ; Na+-NQR ; Na+-translocating NADH ; quinone oxidoreductase ; Rf ; riboflavin ; Q8 ; ubiquinone-8 ; Δμ̅Na+ ; ; transmembrane electrochemical Na+ potential ; Δψ ; transmembrane difference in electric potentials
- 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：1857
- 期：2
- 页码：141-149
- 全文大小：1464 K
文摘
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Vibrio harveyi NADH:quinone oxidoreductase (Na+-NQR) is a primary Na+ pump.
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10">Six steps of Na+-NQR reduction by NADH were resolved in time in a stopped-flow study.
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15">Na+-NQR apparently couples tight Na+ binding with Cys4[Fe] center reduction.
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Electron transfer in Na+-NQR may proceed via an alternating access mechanism.