EMDB/PDB/SASBDBから引用されている文献のデータベース

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構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
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IF	>30 >20 >10 >5 all

タイトル	Cryo-EM structure and kinetics reveal electron transfer by 2D diffusion of cytochrome in the yeast III-IV respiratory supercomplex.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 118, Issue 11, Year 2021
掲載日	2021年3月16日
著者	Agnes Moe / Justin Di Trani / John L Rubinstein / Peter Brzezinski /
PubMed 要旨	Energy conversion in aerobic organisms involves an electron current from low-potential donors, such as NADH and succinate, to dioxygen through the membrane-bound respiratory chain. Electron transfer ...Energy conversion in aerobic organisms involves an electron current from low-potential donors, such as NADH and succinate, to dioxygen through the membrane-bound respiratory chain. Electron transfer is coupled to transmembrane proton transport, which maintains the electrochemical proton gradient used to produce ATP and drive other cellular processes. Electrons are transferred from respiratory complexes III to IV (CIII and CIV) by water-soluble cytochrome (cyt.) In and some other organisms, these complexes assemble into larger CIIICIV supercomplexes, the functional significance of which has remained enigmatic. In this work, we measured the kinetics of the supercomplex cyt. -mediated QH:O oxidoreductase activity under various conditions. The data indicate that the electronic link between CIII and CIV is confined to the surface of the supercomplex. Single-particle electron cryomicroscopy (cryo-EM) structures of the supercomplex with cyt. show the positively charged cyt. bound to either CIII or CIV or along a continuum of intermediate positions. Collectively, the structural and kinetic data indicate that cyt. travels along a negatively charged patch on the supercomplex surface. Thus, rather than enhancing electron transfer rates by decreasing the distance that cyt. must diffuse in three dimensions, formation of the CIIICIV supercomplex facilitates electron transfer by two-dimensional (2D) diffusion of cyt. This mechanism enables the CIIICIV supercomplex to increase QH:O oxidoreductase activity and suggests a possible regulatory role for supercomplex formation in the respiratory chain.
リンク	Proc Natl Acad Sci U S A / PubMed:33836592 / PubMed Central
手法	EM (単粒子)
解像度	3.7 - 5.9 Å
構造データ	EMDB-23414: yeast III-IV supercomplex, III2IV1 local refinement 手法: EM (単粒子) / 解像度: 3.7 Å EMDB-23416: Locally filtered map of yeast III-IV supercomplex with cytochrome c 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-23417: Cytochrome c bound to CIII from yeast III-IV supercomplex. Local non-uniform refinement of CIII-cytochrome c portion, locally filtered. 手法: EM (単粒子) / 解像度: 4.3 Å EMDB-23418: Cytochrome c bound in-between CIII and CIV in yeast III-IV supercomplex. Non-uniform refinement, Locally filtered. 手法: EM (単粒子) / 解像度: 4.3 Å EMDB-23419: Cytochrome c bound to CIV in yeast III-IV supercomplex. Local non-uniform refinement of CIV-cytochrome c portion, locally filtered. 手法: EM (単粒子) / 解像度: 4.7 Å EMDB-23420: CIII2CIV2 yeast supercomplex with cytochrome c. Non-uniform refinement. 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-23421: Yeast CIII2CIV1 supercomplex with cytochrome c 手法: EM (単粒子) / 解像度: 5.9 Å EMDB-23422: Local non-uniform refinement of CIV from yeast III-IV supercomplex 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-23423: Local non-uniform refinement of CIII from yeast III-IV supercomplex 手法: EM (単粒子) / 解像度: 3.7 Å
由来	Saccharomyces cerevisiae (パン酵母)