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  • Rhodobacter capsulatus  (6)
  • MAN/SYSTEM TECHNOLOGY AND LIFE SUPPORT  (4)
  • 1
    Publication Date: 2019-06-28
    Description: Previous design efforts of a cost effective and reliable regenerative life support system (RLSS) provided the foundation for the characterization of organisms or 'biological processors' in engineering terms and a methodology was developed for their integration into an engineered ecological LSS in order to minimize the mass flow imbalances between consumers and producers. These techniques for the design and the evaluation of bioregenerative LSS have now been integrated into a lunar base reference mission, emphasizing the phased implementation of components of such a BLSS. In parallel, a designers handbook was compiled from knowledge and experience gained during past design projects to aid in the design and planning of future space missions requiring advanced RLSS technologies. The lunar base reference mission addresses in particular the phased implementation and integration of BLS parts and includes the resulting infrastructure burdens and needs such as mass, power, volume, and structural requirements of the LSS. Also, operational aspects such as manpower requirements and the possible need and application of 'robotics' were addressed.
    Keywords: MAN/SYSTEM TECHNOLOGY AND LIFE SUPPORT
    Type: NASA-CR-189973 , NAS 1.26:189973
    Format: application/pdf
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  • 2
    Publication Date: 2019-06-28
    Description: The results are described of an effort to establish commonality and standardization of generic crew extravehicular (crew-EVA) and telerobotic task analysis primitives used for the study of spaceborne operations. Although direct crew-EVA plans are the most visible output of spaceborne operations, significant ongoing efforts by a wide variety of projects and organizations also require tools for estimation of crew-EVA and telerobotic times. Task analysis tools provide estimates for input to technical and cost tradeoff studies. A workshop was convened to identify the issues and needs to establish a common language and syntax for task analysis primitives. In addition, the importance of such a syntax was shown to have precedence over the level to which such a syntax is applied. The syntax, lists of crew-EVA and telerobotic primitives, and the data base in diskette form are presented.
    Keywords: MAN/SYSTEM TECHNOLOGY AND LIFE SUPPORT
    Type: NASA-CR-187429 , JPL-PUBL-90-10 , NAS 1.26:187429
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  • 3
    Publication Date: 2019-07-13
    Description: As part of the NASA Controlled Ecological Life Support System (CELSS) Program, a CELSS Test Facility (CTF) is being planned for installation on the Space Station. The CTF will be used to provide data on the productivity and efficiency of a variety of CELSS higher plant crops grown in the microgravity environment of the Space Station. Tight environmental control will be maintained while data on gas exchange rates and biomass accumulation rates are collected. In order to obtain an early realistic determination of the subsystem and system requirements necessary to provide the environmental conditions specified for CTF crop productivity experiments, an Engineering Development Unit (EDU) has been designed, constructed and is in the process of subsystem and system testing at NASA Ames Research Center. The EDU is a ground test-bed which will be used to characterize the integrated performance of major subsystem technologies, to evaluate hardware candidates and control strategies required for the CTF, and to further define the ability to meet CTF requirements within present Space Station constraints. This paper reviews the functional requirements for the EDU, and focuses on the performance evaluation and test results of the various subsystems. Preliminary integrated performance results and control system operation are addressed, and plans for future science and technology testing are discussed.
    Keywords: MAN/SYSTEM TECHNOLOGY AND LIFE SUPPORT
    Type: SAE PAPER 941542 , (ISSN 0148-7191); 7 p.|SAE, International Conference on Environmental Systems; Jun 20, 1994 - Jun 23, 1994; Friedrichshafen; Germany
    Format: text
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  • 4
    Publication Date: 2019-07-13
    Description: The NASA Controlled Ecological Life Support System (CELSS) Program has the goal of developing life support systems for humans in space based on the use of higher plants. The program has supported research at universities with a primary focus of increasing the productivity of candidate crop plants. To understand the effects of the space environment on plant productivity, the CELSS Test Facility (CTF) has been developed as an instrument that will permit the evaluation of plant productivity on Space Station Freedom. The CFT will maintain specific environmental conditions and collect data on gas exchange rates and biomass accumulation over the growth period of several crop plants grown sequentially from seed to harvest. To better understand the systems needed to support plants and maintain the evironmental conditions required by CTF, an Engineering Development Unit (EDU) is being constructed at NASA Ames Research Center (ARC) in the Advanced Life Support Division. The EDU will provide the means of testing and evaluating hardware solutions to CTF requirements. This paper reviews the CTF science and functional requirements, and provides a description of the EDU objectives, design approach, subsystem descriptions, and some of the technology tools employed in accomplishing the design.
    Keywords: MAN/SYSTEM TECHNOLOGY AND LIFE SUPPORT
    Type: SAE PAPER 932124 , International Conference on Environmental Systems; Jul 12, 1993 - Jul 15, 1993; Colorado Springs, CO; United States|(ISSN 0148-7191); 9 p.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 156 (1991), S. 129-134 
    ISSN: 1432-072X
    Keywords: δ-Aminolevulinic acid synthase ; Bacteriochlorophyll ; Promoter activity ; Oxygen regulation ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The promoter of the Rhodobacter capsulatus hemA gene, coding for the enzyme δ-aminolevulinic acid synthase (ALAS), was identified by trans-complementation of a δ-aminolevulinic acid (ALA)-dependent mutant and found to be located within a 170 bp region proximal to the hemA gene. The activity of the hemA promoter was demonstrated by lacZ fusion and in vitro transcription-translation. An open reading frame (ORFX) was found downstream of hemA. The activity of the hemA promoter, but not that of the ORFX promoter, increased when oxygen tension was lowered in the culture. Deletions upstream of the hemA promoter region did not affect ALAS activity and formation of pigment-protein complexes in R. capsulatus.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 149 (1987), S. 12-18 
    ISSN: 1432-072X
    Keywords: Oxidase regulation ; Cytochrome c oxidase ; Cytochrome c 2 ; Regulatory DNA sequence ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to distinguish between the regulatory effects of oxygen tension and light intensity on cytochrome c oxidase protein and enzymatic activity cells of Rhodobacter capsulatus were shifted from phototrophic (anaerobic, light) growth to aerobic-light, aerobic-dark and to anaerobic-dark conditions, respectively. During shift-experiments the formation of oxidase protein and regulation of oxidase activity was followed by immunological and enzymatic means. The results support the idea, that the formation of oxidase protein is regulated by oxygen tension and light intensity changes, whereas the regulation of oxidase activity seems only to be correlated to the oxygen tension. A DNA sequence involved in the oxygen-dependent regulation of cytochrome oxidase could be identified in the regulation-deficient oxidase mutant H41 of R. capsulatus. Immunological investigations of cytochrome c 2 from mutant H41 demonstrated at the same time the participation of the c 2-polypeptide in the regulation of cytochrome c oxidase.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-072X
    Keywords: Protein phosphorylation ; Antenna protein ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Labelling of Rhodobacter capsulatus cells with (32P)Pi in a phototrophic culture results in phosphorylation of a membrane-bound polypeptide identified as the α subunit of the LHI antenna complex of the photosynthetic apparatus. Phosphorylation of the same polypeptide was also observed by incubation of chromatophores with (32P)ATP or under conditions of photophosphorylation with ADP and (32P)Pi. The identity of the phosphorylated LHI-α subunit was demonstrated by N-terminal protein sequencing of the phosphorylated polypeptide and by failure of labelling in LHI-defective mutants. Pre-aeration of the samples or addition of the oxidant potassium ferrcyanide stimulated the kinase activity whereas the presence of soluble cytoplasmic proteins impaired phosphorylation in an in vitro assay. No effect resulted from addition of reductants to the assay medium. The results indicate the presence of a membrane-bound protein kinase in R. capsulatus that phosphorylates the α subunit of the LHI antenna complex under redox control.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0014-5793
    Keywords: LHI α polypeptide ; Membrane insertion ; Rhodobacter capsulatus ; Signal peptide ; Site-directed mutagenesis
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-5079
    Keywords: light-harvesting complex I ; Rhodobacter capsulatus ; chaperone DnaK ; GroEL ; membrane insertion ; cell-free translation system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Transcripts of the genes pufBA, pufB or pufA from Rhodobacter capsulatus were translated in a cell-free system of R. capsulatus. The incorporation of the nascent polypeptides LHIα and β in various types of membranes and the assembly of the light-harvesting (LH) complex I (B870) were investigated. The highest rate of stable incorporation of LHIα and β into the membrane was observed with membranes from the wild type strain grown under chemotrophic conditions. Addition of membranes from cells defective in biosynthesis of pigment-binding proteins resulted in a less efficient or less stable incorporation of LHIαβ. The single polypeptides LHIα or β were synthesized and inserted into the membrane but were extractable to a higher percentage by 6 M urea than the pairwise inserted LHI polypeptides. If the ribosomes and the S135 extract were depleted of DnaK the rate of synthesis of both polypeptides, LHIα and β, was strongly reduced. Removal of GroEL from the cell-free system did not impair the synthesis and membrane association of both proteins, but affected the stable insertion. A high percentage of the LHIαβ polypeptides became extractable by 6 M urea if the cell-free system was depleted of GroEL. Addition of GroEL to the cell-free system restored the capacity of stable insertion of both proteins into the membrane. GroEL interacted with LHIα and β before membrane targeting as shown by immunological means. A protein fraction, which can be removed from the membrane with a low-salt buffer, supported the effective and stable incorporation of LHIαβ into the membrane. It is concluded that the assembly of the LHI complex in the membrane system of R. capsulatus is a multistep process guided and supported by polypeptides located in the cytoplasm and in the membrane. In the cell-free in vitro system not only the correct insertion of the LHI polypeptides but also an assembly with bacteriochlorophyll was observed. BChl was synthesized from δ-amino levulinate in the cell free system.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1617-4623
    Keywords: hemA ; δ-Aminolevulinic acid synthase ; Tetrapyrrole biosynthesis ; Phototrophic bacteria ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Rhodobacter capsulatus hemA gene, coding for the enzyme δ-aminolevulinic acid synthase (ALAS), was isolated from a genome bank by hybridization with a hemT probe from Rhodobacter sphaeroides. Subcloning of the initial 3.9 kb HindIII fragment allowed the isolation of a 2.5 kb HindIII-BglII fragment which was able to complement the δ-aminolevulinic acid-requiring (ALA-requiring) Escherichia coli mutant SHSP19. DNA sequencing revealed an open reading frame coding for a protein with 401 amino acids which displayed similarity to the amino acid sequences of other known ALASs. However, no resemblance was seen to the HemA protein of E. coli K12. Based on the sequence data, an ALA-requiring mutant strain of R. capsulatus was constructed by site-directed insertion mutagenesis. Introduction of a plasmid, containing the hemA gene of R. capsulatus on the 3.9 kb HindIII fragment, restored ALA-independent growth of the mutant indicating that there is only one gene for ALA biosynthesis in R. capsulatus. Transfer of the R′ factor pRPS404 and hybridization analysis revealed that the ALAS gene is not located within the major photosynthetic gene cluster.
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