Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I
Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I
复制标题
半胱氨酸扫描显示呼吸复合物 I 水平螺旋的微小局部重排
DOI:
10.1111/mmi.13112
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发表时间:
2015
影响因子:
3.6
通讯作者:
Friedrich
中科院分区:
文献类型:
--
作者:
Steimle;Schnick;Burger;Krämer;Dawitz;Brander;Matlosz;Schäfer;Maurer;Glessner;Friedrich
The NADH:ubiquinone oxidoreductase, respiratory complex I, couples electron transfer from NADH to ubiquinone with the translocation of protons across the membrane. The complex consists of a peripheral arm catalyzing the redox reaction and a membrane arm catalyzing proton translocation. The membrane arm is almost completely aligned by a 110 Å unique horizontal helix that is discussed to transmit conformational changes induced by the redox reaction in a piston‐like movement to the membrane arm driving proton translocation. Here, we analyzed such a proposed movement by cysteine‐scanning of the helix of theEscherichia colicomplex I. The accessibility of engineered cysteine residues and the flexibility of individual positions were determined by labeling the preparations with a fluorescent marker and a spin‐probe, respectively, in the oxidized and reduced states. The differences in fluorescence labeling and the rotational flexibility of the spin probe between both redox states indicate only slight conformational changes at distinct positions of the helix but not a large movement.
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影响因子:
5.7
作者:
L. Sazanov
通讯作者:
L. Sazanov
影响因子:
5.6
作者:
Baranova, Ekaterina A.;Holt, Peter J.;Sazanov, Leonid A.
通讯作者:
Sazanov, Leonid A.
影响因子:
56.9
作者:
Zickermann, Volker;Wirth, Christophe;Brandt, Ulrich
通讯作者:
Brandt, Ulrich
DOI:
10.1073/pnas.120163297
发表时间:
2000-06-06
影响因子:
11.1
作者:
Datsenko, KA;Wanner, BL
通讯作者:
Wanner, BL
影响因子:
2.9
作者:
Steimle, Stefan;Bajzath, Csaba;Friedrich, Thorsten
通讯作者:
Friedrich, Thorsten