![]() This large membrane protein complex is composed of up to ∼45 subunits in mammals with a total molecular weight approaching 1 MDa. ![]() The cyanobacterial and chloroplast type I NADPH dehydrogenase (NDH-1) complex is structurally and functionally related to the energy-converting NAD(P)H:Quinone oxidoreductase (Complex I) – one key-enzyme of the energy metabolism in eubacteria (like Escherichia coli) and the respiratory chain of mitochondria –. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist. All relevant data are within the paper and its Supporting Information files.įunding: This work was supported by the RUB Research School (HW) and by grants of the Deutsche Forschungsgemeinschaft (HW and MMN) and the BioSolar Cells project (LEF and EJB). This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.ĭata Availability: The authors confirm that all data underlying the findings are fully available without restriction. Received: ApAccepted: JPublished: August 13, 2014Ĭopyright: © 2014 Wulfhorst et al. PLoS ONE 9(8):Įditor: Andrew Webber, Arizona State University, United States of America Moreover, NdhP is essential for NDH-1L formation, as this type of NDH-1 was not detectable in a Δ ndhP::Km mutant.Ĭitation: Wulfhorst H, Franken LE, Wessinghage T, Boekema EJ, Nowaczyk MM (2014) The 5 kDa Protein NdhP Is Essential for Stable NDH-1L Assembly in Thermosynechococcus elongatus. C-terminal fusion of NdhP with his-tagged superfolder GFP and the subsequent analysis of the purified complex by electron microscopy and single particle averaging revealed its localization in the NDH-1L specific distal unit of the NDH-1 complex, that is formed by the subunits NdhD1 and NdhF1. Here we show that NdhP is a unique component of the ∼450 kDa NDH-1L complex, that is involved in respiration and CET at high CO 2 concentration, and not detectable in the NDH-1MS and NDH-1MS' complexes that play a role in carbon concentration. We have recently discovered in a NDH-1 preparation from Thermosynechococcus elongatus two novel single transmembrane peptides (NdhP, NdhQ) with molecular weights below 5 kDa. Despite many achievements in the past, the complex protein composition and the specific function of many subunits of the different NDH-1 species remain elusive. Sericitic alteration in quartz-feldspar porphyry.The cyanobacterial NADPH:plastoquinone oxidoreductase complex (NDH-1), that is related to Complex I of eubacteria and mitochondria, plays a pivotal role in respiration as well as in cyclic electron transfer (CET) around PSI and is involved in a unique carbon concentration mechanism (CCM). The Fairview prospect has a 40Ar/39Ar age of 72.6 Ma (Gray, Gent, and others, 1997). Silica-carbonate mercury (Cox and Singer, 1986 model 27c). ![]() One 50-foot zone in trench 1 averaged 0.15 percent mercury one 5-foot zone in trench 2 averaged 0.40 percent mercury. Bureau of Mines (Webber and others (1947). In the early 1940s, three trenches were sampled by the U.S. The Fairview deposit has a 40Ar/39Ar isochron age of 72.6 Ma (Gray, Gent, and others, 1997) it is the only mercury deposit in the Red Devil area that has been dated.The mineralization consists of cinnabar, stibnite, and quartz that fills several parallel fractures in the central part of the altered felsic sill. The host rock is an altered, sericitized, quartz-feldspar-porphyry sill about 120 feet thick and 1,000 feet long that trends northwest, parallel to the strike of the shale and sandstone of the Upper Cretaceous, Kuskokwim Group that contains the sill (Cady and others, 1955 Sainsbury and MacKevett, 1965). ![]() The Fairview prospect is unusual because it is one of the few cinnabar prospects in the Kuskokwim mineral belt that is wholly in intrusive rock.
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