Acidianus ambivalens Complex II Typifies a Novel Family of Succinate Dehydrogenases

Lemos, Rita S.; Gomes, Cláudio M.; Teixeira, Miguel

doi:10.1006/bbrc.2001.4317

Cited by 37 publications

(26 citation statements)

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“…The Msed1540s region is not predicted to contain transmembrane proteins, but the methanogen Hdr complex activity has been found in the membrane following gentle disruption (49). Alternative considerations should include association of the Hdr complex with other transmembrane proteins outside the gene neighborhood or the possibility that some Hdr-associated subunits may be integral membrane proteins containing amphipathic helices not predicted with TMM software, as seen in the HdrB-like SucC sequence from A. ambivalens (32).…”

Section: Discussionmentioning

confidence: 99%

“…1 and Table 1). Based on studies in Acidianus ambivalens, Sulfolobus metallicus, and Sulfolobus tokodaii (3,17,24,32,40), electrons from NADH or succinate oxidation presumably enter ETC via NADH:quinone oxidoreductases (NDH-II enzymes) or succinate:quinone oxidoreductases (SdhABCD; type E). Reduced quinones (typically caldariella or Sulfolobus-type quinones) then deliver electrons to one of several terminal oxidase complexes, composed of cytochrome oxidase and/or bc 1 complex-like subunits.…”

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confidence: 99%

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Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes

Auernik

Kelly

2008

Appl Environ Microbiol

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The crenarchaeal order Sulfolobales collectively contain at least five major terminal oxidase complexes. Based on genome sequence information, all five complexes are found only in Metallosphaera sedula and Sulfolobus tokodaii, the two sequenced Sulfolobales capable of iron oxidization. While specific respiratory complexes in certain Sulfolobales have been characterized previously as proton pumps for maintaining intracellular pH and generating proton motive force, their contribution to sulfur and iron biooxidation has not been considered. For M. sedula growing in the presence of ferrous iron and reduced inorganic sulfur compounds (RISCs), global transcriptional analysis was used to track the response of specific genes associated with these complexes, as well as other known and putative respiratory electron transport chain elements. Open reading frames from all five terminal oxidase or bc 1 -like complexes were stimulated on one or more conditions tested. Components of the fox (Msed0467 to Msed0489) and soxNL-cbsABA (Msed0500 to Msed0505) terminal/quinol oxidase clusters were triggered by ferrous iron, while the soxABCDD terminal oxidase cluster (Msed0285 to Msed0291) were induced by tetrathionate and S 0 . Chemolithotrophic electron transport elements, including a putative tetrathionate hydrolase (Msed0804), a novel polysulfide/sulfur/dimethyl sulfoxide reductase-like complex (Msed0812 to Msed0818), and a novel heterodisulfide reductase-like complex (Msed1542 to Msed1550), were also stimulated by RISCs. Furthermore, several hypothetical proteins were found to have strong responses to ferrous iron or RISCs, suggesting additional candidates in iron or sulfur oxidation-related pathways. From this analysis, a comprehensive model for electron transport in M. sedula could be proposed as the basis for examining specific details of iron and sulfur oxidation in this bioleaching archaeon.Certain extremely thermoacidophilic archaea are promising candidates for biomining operations targeting the recovery of base and precious metals (44). These microorganisms grow at elevated temperatures where abiotic ferrous oxidation rates are accelerated and where passivation of mineral surfaces from reduced inorganic sulfur compounds (RISCs) is minimal (44). To tap into the biotechnological potential of these microorganisms, their physiological characteristics that relate to metal mobilization need to be better understood, especially mechanisms underlying biooxidation of iron (Fe 2ϩ ) and RISCs. Biooxidation implicates membrane-associated protein complexes that mediate electron transport, which seemingly determines the capability and capacity of extreme thermoacidophiles for metal and sulfur mobilization. However, the complexes required for bioleaching have not been established. Models that address the specific and collective function of electron transport complexes in the Sulfolobales are needed to provide a physiological framework for exploring the intricacies of biological metal and sulfur oxidation.Current knowledge of respiratory el...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes

Auernik

Kelly

2008

Appl Environ Microbiol

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“…The simplest method of membrane anchoring involves one transmembrane ␣-helix traversing the membrane once, in contrast to the case where several ␣-helices or ␤-strands pass through the bilayer several times. An alternative strategy for membrane anchoring of proteins uses ␣-helices parallel to the plane of the membrane, which are sometimes amphipathic, with, in this case, predominantly polar residues along one side of the helix and nonpolar side chains on the remainder opposite the helical structure, as observed in several enzymes such as prostaglandin synthase (9,74) and proposed for type E succinate:quinone oxidoreductases (37). The anchoring of NDH-2 to the membrane remains controversial, since transmembrane helices are not commonly present among NDH-2 proteins.…”

Section: Analyses Of Ndh-2 Primary Structuresmentioning

confidence: 99%

New Insights into Type II NAD(P)H:Quinone Oxidoreductases

Melo

Bandeiras

Teixeira

2004

Microbiol Mol Biol Rev

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238

212

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Type II NAD(P)H:quinone oxidoreductases (NDH-2) catalyze the two-electron transfer from NAD(P)H to quinones, without any energy-transducing site. NDH-2 accomplish the turnover of NAD(P)H, regenerating the NAD(P)+ pool, and may contribute to the generation of a membrane potential through complexes III and IV. These enzymes are usually constituted by a nontransmembrane polypeptide chain of ∼50 kDa, containing a flavin moiety. There are a few compounds that can prevent their activity, but so far no general specific inhibitor has been assigned to these enzymes. However, they have the common feature of being resistant to the complex I classical inhibitors rotenone, capsaicin, and piericidin A. NDH-2 have particular relevance in yeasts like Saccharomyces cerevisiae and in several prokaryotes, whose respiratory chains are devoid of complex I, in which NDH-2 keep the [NADH]/[NAD+] balance and are the main entry point of electrons into the respiratory chains. Our knowledge of these proteins has expanded in the past decade, as a result of contributions at the biochemical level and the sequencing of the genomes from several organisms. The latter showed that most organisms contain genes that potentially encode NDH-2. An overview of this development is presented, with special emphasis on microbial enzymes and on the identification of three subfamilies of NDH-2

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“…The respiratory chain of Sulfolobales species contains type II NADH dehydrogenase Schäfer, 1996;Schäfer et al, 1996) and a novel family of succinate dehydrogenase (Gomes et al, 1999;Iwasaki et al, 1995c;Janssen et al, 1997;Lemos et al, 2001). In addition Sulfolobus acidocaldarius and S. tokodaii have alternative electron carriers for cytochrome c such as sulfocyanin or cytochrome a (Gleißner et al, 1997;Iwasaki et al, 1995b;Schäfer, 1996;Lübben et al, 1992).…”

Section: Overview Of the Aerobic Respiratory Chainmentioning

confidence: 99%

Regulation of the aerobic respiratory chain in the facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense

et al. 2003

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Acidianus ambivalens Complex II Typifies a Novel Family of Succinate Dehydrogenases

Cited by 37 publications

References 49 publications

Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes

Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes

New Insights into Type II NAD(P)H:Quinone Oxidoreductases

Regulation of the aerobic respiratory chain in the facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense

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