title: NDH-1L interacts with ferredoxin via the subunit NdhS in Thermosynechococcus elongatus.
abstract: The large size complex of cyanobacterial NAD(P)H dehydrogenase (NDH-1) complex (NDH-1L) plays crucial role in a variety of bioenergetic reactions such as respiration and cyclic electron flow around photosystem I. Although the complex has been isolated and identified, its biochemical function still remains to be clarified. Here, we highly purified the NDH-1L complex from the cells of Thermosynechococcus elongatus by Ni(2+) affinity chromatography and size-exclusion chromatography. The purified NDH-1L complex has an apparent total molecular mass of approximately 500 kDa. 14 known subunits were identified by mass spectrometry and immunoblotting, including the NdhS subunit containing ferredoxin (Fd)-docking site domain. Surface plasmon resonance measurement demonstrates that the NDH-1L complex could bind to Fd with the binding constant (K D) of 59 µM. Yeast two-hybrid system assay further confirmed the interaction of Fd with NdhS and indicated that NdhH is involved in the interaction. Our results provide direct biochemical evidence that the cyanobacterial NDH-1 complex catalyzes the electron transport from reduced Fd to plastoquinone via NdhS and NdhH.
authors: National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 300 Fenglin Road, Shanghai, 200032, China.
authors: Zhihui
authors: Z
authors: He
authors: National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 300 Fenglin Road, Shanghai, 200032, China.
authors: Fangfang
authors: F
authors: Zheng
authors: National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 300 Fenglin Road, Shanghai, 200032, China.
authors: Yaozong
authors: Y
authors: Wu
authors: National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 300 Fenglin Road, Shanghai, 200032, China.
authors: Qinghua
authors: Q
authors: Li
authors: Renewable Energy Research Center, China University of Petroleum Beijing, 18 Fuxue Road, Changping, Beijing, 102249, China.
authors: Jing
authors: J
authors: Lv
authors: Renewable Energy Research Center, China University of Petroleum Beijing, 18 Fuxue Road, Changping, Beijing, 102249, China.
authors: Pengcheng
authors: P
authors: Fu
authors: National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 300 Fenglin Road, Shanghai, 200032, China. mihl@sippe.ac.cn.
authors: Hualing
authors: H
authors: Mi
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D000458:Cyanobacteria / Q000378:metabolism*; D004579:Electron Transport; D005288:Ferredoxins / Q000378:metabolism*; D009252:NADPH Dehydrogenase / Q000378:metabolism*; D045331:Photosystem I Protein Complex / Q000378:metabolism; D010971:Plastoquinone / Q000378:metabolism; D021122:Protein Subunits
chemical_list: D001426:Bacterial Proteins; D005288:Ferredoxins; D045331:Photosystem I Protein Complex; D021122:Protein Subunits; D009252:NADPH Dehydrogenase; D010971:Plastoquinone
keywords: Cyanobacteria; Ferredoxin; NDH-1 complex; Purification; Surface plasmon resonance; Thermosynechococcus elongatus
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