bacteriopheophytin and dodecyldimethylamine-oxide

bacteriopheophytin has been researched along with dodecyldimethylamine-oxide* in 2 studies

Other Studies

2 other study(ies) available for bacteriopheophytin and dodecyldimethylamine-oxide

Article	Year
[Influence of LDAO on the conformation and release of bacteriochlorophyll of peripheral light-harvesting complex (LH2) from Rhodobacter azotoformans]. Guang pu xue yu guang pu fen xi = Guang pu, 2010, Volume: 30, Issue:10 The aim of this study is to reveal the interaction relationships between lauryl dimethylamine N-oxide (LDAO) and peripheral light-harvesting complex (LH2) as well as the influence of LDAO on structure and function of LH2. In the present work, the effects of LDAO on the conformation and release processes of bacteriochlorophyll (BChl) of LH2 when incubated under different temperature and pH in the presence and absence of LDAO were investigated by spectroscopy. The results indicated that (1) the presence of LDAO resulted in alterations in the conformation, alpha-helix content, and spectra of Tyr and B850 band of LH2 at room temperature and pH 8.0. Moreover, energy transfer efficiency of LH2 was enhanced markedly in the presence of LDAO. (2) At 60 degrees C, both the B800 and B850 band of LH2 were released and transited into free BChl at pH 8.0. However, the release rates of bacteriochlorophylls of B800 and B850 band from LH2 were slowed down and the release processes were changed when incubated in the presence of LDAO. Hence, the stability of LH2 was improved in the presence of LDAO. (3) The accelerated release processes of bacteriochlorophylls of B800 and B850 band of LH2 were induced to transform into bacteriopheophytin (BPhe) and free BChl by LDAO in strong acid and strong alkalic solution at room temperature. However, the kinetic patterns of the B800 and B850 band were remarkably different. The release and self-assemble processes of B850 in LH2 were observed in strong acid solution without LDAO. Therefore, the different release behaviors of B800 and B850 of LH2 are induced by LDAO under different extreme environmental conditions. Topics: Bacterial Proteins; Bacteriochlorophylls; Dimethylamines; Energy Transfer; Kinetics; Light-Harvesting Protein Complexes; Pheophytins; Protein Structure, Secondary; Rhodobacter	2010
Physicochemical properties of detergent-solubilized photochemical reaction centers from two strains of Rhodopseudomonas spheroides. Biochemistry, 1980, Jun-24, Volume: 19, Issue:13 Topics: Bacterial Proteins; Bacteriochlorophylls; Dimethylamines; Iron; Light-Harvesting Protein Complexes; Mathematics; Molecular Weight; Pheophytins; Phospholipids; Photosynthetic Reaction Center Complex Proteins; Protein Binding; Protein Conformation; Rhodobacter sphaeroides; Ubiquinone	1980

Article

Year

[Influence of LDAO on the conformation and release of bacteriochlorophyll of peripheral light-harvesting complex (LH2) from Rhodobacter azotoformans].

Guang pu xue yu guang pu fen xi = Guang pu, 2010, Volume: 30, Issue:10

The aim of this study is to reveal the interaction relationships between lauryl dimethylamine N-oxide (LDAO) and peripheral light-harvesting complex (LH2) as well as the influence of LDAO on structure and function of LH2. In the present work, the effects of LDAO on the conformation and release processes of bacteriochlorophyll (BChl) of LH2 when incubated under different temperature and pH in the presence and absence of LDAO were investigated by spectroscopy. The results indicated that (1) the presence of LDAO resulted in alterations in the conformation, alpha-helix content, and spectra of Tyr and B850 band of LH2 at room temperature and pH 8.0. Moreover, energy transfer efficiency of LH2 was enhanced markedly in the presence of LDAO. (2) At 60 degrees C, both the B800 and B850 band of LH2 were released and transited into free BChl at pH 8.0. However, the release rates of bacteriochlorophylls of B800 and B850 band from LH2 were slowed down and the release processes were changed when incubated in the presence of LDAO. Hence, the stability of LH2 was improved in the presence of LDAO. (3) The accelerated release processes of bacteriochlorophylls of B800 and B850 band of LH2 were induced to transform into bacteriopheophytin (BPhe) and free BChl by LDAO in strong acid and strong alkalic solution at room temperature. However, the kinetic patterns of the B800 and B850 band were remarkably different. The release and self-assemble processes of B850 in LH2 were observed in strong acid solution without LDAO. Therefore, the different release behaviors of B800 and B850 of LH2 are induced by LDAO under different extreme environmental conditions.

Topics: Bacterial Proteins; Bacteriochlorophylls; Dimethylamines; Energy Transfer; Kinetics; Light-Harvesting Protein Complexes; Pheophytins; Protein Structure, Secondary; Rhodobacter

2010

Physicochemical properties of detergent-solubilized photochemical reaction centers from two strains of Rhodopseudomonas spheroides.

Biochemistry, 1980, Jun-24, Volume: 19, Issue:13

Topics: Bacterial Proteins; Bacteriochlorophylls; Dimethylamines; Iron; Light-Harvesting Protein Complexes; Mathematics; Molecular Weight; Pheophytins; Phospholipids; Photosynthetic Reaction Center Complex Proteins; Protein Binding; Protein Conformation; Rhodobacter sphaeroides; Ubiquinone

1980