ArticleJournal of bioenergetics and biomembranes2001
A new type-II NADH dehydrogenase from the archaeon Acidianus ambivalens: characterization and in vitro reconstitution of the respiratory chain.
Article in Journal of bioenergetics and biomembranes, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 39 citations in OpenAlex.
- Intersection of Biotic and Abiotic Sulfur Chemistry Supporting Extreme Microbial Life in Hot Acid.The journal of physical chemistry. B · 2021Article
- A comparative genomics perspective on the genetic content of the alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.BMC genomics · 2012Article
- Characterization of growth and metabolism of the haloalkaliphile Natronomonas pharaonis.PLoS computational biology · 2010Article
- Type II NADH dehydrogenase of the respiratory chain of Plasmodium falciparum and its inhibitors.Bioorganic & medicinal chemistry letters · 2009Article
- Identification of components of electron transport chains in the extremely thermoacidophilic crenarchaeon Metallosphaera sedula through iron and sulfur compound oxidation transcriptomes.Applied and environmental microbiology · 2008Article
- Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4.Biochimica et biophysica acta · 2008Article
- Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.Genome research · 2005Article
- New insights into type II NAD(P)H:quinone oxidoreductases.Microbiology and molecular biology reviews : MMBR · 2004Review
- Dissimilatory oxidation and reduction of elemental sulfur in thermophilic archaea.Journal of bioenergetics and biomembranes · 2004Review
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3 authors at 1 institution in 1 country.
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Abstract
A new type-II NADH dehydrogenase (NDH-II) was isolated from the hyperthermoacidophilic archaeon Acidianus ambivalens. This enzyme is a monomer with an apparent molecular mass of 47 kDa, containing a covalently bound flavin, and no iron-sulfur clusters. Upon isolation, NDH-II loses activity, which can, nevertheless, be restored by incubation with phospholipids. Catalytically, it is a proficient NADH:caldariella quinone oxidoreductase (130 mmol NADH oxidized/mg protein(-1)/min(-1)) but it can also donate electrons to synthetic quinones, strongly suggesting its involvement in the respiratory chain. The apparent Km for NADH was found to be approximately 6 microM, both for the purified and membrane-integrated enzyme, thus showing that detergent solubilization and purification did not affect the substrate binding site. Further, it is the first example of a type-II NADH dehydrogenase that contains the flavin covalently attached, which may be related to the need to stabilize the otherwise labile cofactor in a thermophilic environment. A fully operative minimal version of Acidianus ambivalens respiratory system was successfully reconstituted into artificial liposomes, using three basic components isolated from the organism: the type-II NADH dehydrogenase, caldariella quinone, the organism-specific quinone, and the aa3 type quinol oxidase. This system, which mimics the in vivo chain, is efficiently energized by NADH, driving oxygen consumption by means of the terminal oxidase.
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