• 대한의생명과학회지
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• 제14권2호
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• pp.91-96
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• 2008

Light Emitting Diode (LED) of 880 nm was used as a function of luminosity in culture of the photosynthetic bacteria including Rhodobacter sp.. An array of 880 run LED was driven with an energy density of $6.0mW/cm^2$. In processing time, we were able to show that the cell growth were gained of significant changes in the pigment and in the dry weight. And we also showed that photosynthetic bacteria had the resonable relativity of optical density to dry weight. LED-880nm is of great significance for the potential use of photo-bioreactor construction.

• Fisheries and Aquatic Sciences
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• 제11권3호
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• pp.172-176
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• 2008

To develop a potent strain for the production of coenzyme $Q_{10}$, a photosynthetic bacterium was isolated from silt of the Nakdong River in Korea. Using l6S-rDNA sequence analysis, the isolated strain was identified as Rhodobacter sphaeroides. A stable improvement in its $CoQ_{10}$ content was achieved by chemical mutation, upon which the content of $CoQ_{10}$(2.94 mg/g dry cell) was increased by approximately 1.9-fold, comparable to that of R. sphaeroides reported in other studies. The isolate is a potentially valuable microorganism for mass production of $CoQ_{10}$, and may provide an appropriate model for further study of economical mass production.

• 한국미생물생명공학회:학술대회논문집
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• 한국미생물생명공학회 2003년도 2003 Annual Meeting, BioExhibition and International Symposium
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• pp.159-160
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• 2003

• 한국미생물생명공학회:학술대회논문집
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• 한국미생물생명공학회 2000년도 추계 학술대회
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• pp.5-7
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• 2000

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2003년도 제39회 학술심포지움
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• pp.13-18
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• 2003

• 한국동물학회:학술대회논문집
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• 한국동물학회 2000년도 한국생물과학협회 학술발표대회
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• pp.59.1-59
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• 2000

No Abstract, See Full Text

• 한국미생물학회:학술대회논문집
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• 한국미생물학회 2000년도 International Meeting 2000
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• pp.4-8
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• 2000

• 미생물과산업
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• 제14권3호
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• pp.7-11
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• 1988

이글에서는 pet A, B, C에 대한 일차적인 아미노산 배열을 알았고 여기서 우리는 위의 정보들을 토대로하여 R. capsulatus에 대한 site-specific oligonucleotide-directed mutagenesis 등 여러 연구를 할 수가 있을 것이다.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2020년도 추계학술대회
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• pp.38-38
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• 2020

• BMB Reports
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• 제40권5호
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• pp.697-707
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• 2007

Cytochrome $cbb_3$ oxidase is a member of the heme-copper oxidase superfamily that catalyses the reduction of molecular oxygen to the water and conserves the liberated energy in the form of a proton gradient. Comparison of the amino acid sequences of subunit I from different classes of heme-copper oxidases showed that transmembrane helix VIII and the loop between transmembrane helices IX and X contain five highly conserved polar residues; Ser333, Ser340, Thr350, Asn390 and Thr394. To determine the relationship between these conserved amino acids and the activity and assembly of the $cbb_3$ oxidase in Rhodobacter capsulatus, each of these five conserved amino acids was substituted for alanine by site-directed mutagenesis. The effects of these mutations on catalytic activity were determined using a NADI plate assay and by measurements of the rate of oxygen consumption. The consequence of these mutations for the structural integrity of the $cbb_3$ oxidase was determined by SDS-PAGE analysis of chromatophore membranes followed by TMBZ staining. The results indicate that the Asn390Ala mutation led to a complete loss of enzyme activity and that the Ser333Ala mutation decreased the activity significantly. The remaining mutants cause a partial loss of catalytic activity. All of the mutant enzymes, except Asn390Ala, were apparently correctly assembled and stable in the membrane of the R. capsulatus.