The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane‐bound multisubunit hydrogenases

FEBS Letters

Friedrich, Thorsten¹  Scheide, Dierk¹ 

[1] Institut für Biochemie, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, D-40225 Düsseldorf, Germany

关键词: NADH:ubiquinone oxidoreductase;    Complex I;    [NiFe] hydrogenase;    Modular evolution;    Iron–sulfur cluster;    Respiratory chain;    Energy conservation;    F420;    (N-L-lactyl-γ-L-glutamyl)-L-glutamic acid phosphodiester of 7;    8-didemethyl-8-hydroxy-5-deazariboflavin-5′-phosphate;    F420H2;    reduced F420;   

DOI  :  10.1016/S0014-5793(00)01867-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The proton-pumping NADH:ubiquinone oxidoreductase, also called complex I, is the first of the respiratory complexes providing the proton motive force which is essential for energy consuming processes like the synthesis of ATP. Homologues of this complex exist in bacteria, archaea, in mitochondria of eukaryotes and in chloroplasts of plants. The bacterial and mitochondrial complexes function as NADH dehydrogenase, while the archaeal complex works as F₄₂₀H₂ dehydrogenase. The electron donor of the cyanobacterial and plastidal complex is not yet known. Despite the different electron input sites, 11 polypeptides constitute the structural framework for proton translocation and quinone binding in the complex of all three domains of life. Six of them are also present in a family of membrane-bound multisubunit [NiFe] hydrogenases. It is discussed that they build a module for electron transfer coupled to proton translocation.

【 授权许可】

Unknown