quinol oxidase (electrogenic, proton-motive force generating) / oxidoreductase activity, acting on diphenols and related substances as donors / cytochrome complex / aerobic electron transport chain / outer membrane / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / oxidative phosphorylation / electron transfer activity / heme binding / membrane ...quinol oxidase (electrogenic, proton-motive force generating) / oxidoreductase activity, acting on diphenols and related substances as donors / cytochrome complex / aerobic electron transport chain / outer membrane / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / oxidative phosphorylation / electron transfer activity / heme binding / membrane / metal ion binding / plasma membrane 類似検索 - 分子機能
ジャーナル: Nat Commun / 年: 2019 タイトル: Homologous bd oxidases share the same architecture but differ in mechanism. 著者: Alexander Theßeling / Tim Rasmussen / Sabrina Burschel / Daniel Wohlwend / Jan Kägi / Rolf Müller / Bettina Böttcher / Thorsten Friedrich / 要旨: Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus ...Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus contributing to the generation of the protonmotive force. Here, we determine the structure of the Escherichia coli bd oxidase treated with the specific inhibitor aurachin by cryo-electron microscopy (cryo-EM). The major subunits CydA and CydB are related by a pseudo two fold symmetry. The heme b and d cofactors are found in CydA, while ubiquinone-8 is bound at the homologous positions in CydB to stabilize its structure. The architecture of the E. coli enzyme is highly similar to that of Geobacillus thermodenitrificans, however, the positions of heme b and d are interchanged, and a common oxygen channel is blocked by a fourth subunit and substituted by a more narrow, alternative channel. Thus, with the same overall fold, the homologous enzymes exhibit a different mechanism.
名称: bd-oxidase from Escherichia coli / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#4 詳細: Reconstruction into Amphipole A8-35 in the presence of the inhibitor aurachin C.
凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277 K / 装置: FEI VITROBOT MARK IV / 詳細: blot time 3.5 sec, blot force 5.
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電子顕微鏡法
顕微鏡
FEI TITAN KRIOS
撮影
フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 検出モード: COUNTING / 撮影したグリッド数: 1 / 実像数: 8663 / 平均露光時間: 75.0 sec. / 平均電子線量: 59.0 e/Å2 / 詳細: Images were collected in movie mode with 47 frames.