RESONANCE-ENHANCED CARS SPECTROSCOPY OF BILIPROTEINS. INFLUENCE OF AGGREGATION and LINKER PROTEINS ON CHROMOPHORE STRUCTURE IN ALLOPHYCOCYANIN (Mastigocladus laminosus)

2008 ◽  
Vol 62 (5) ◽  
pp. 847-854 ◽  
Author(s):  
S. Schneider ◽  
C.-J. Prenzel ◽  
G. Brehm ◽  
L. Gottschalk ◽  
K.-H. Zhao ◽  
...  
Keyword(s):  
Mastigocladus Laminosus

scholarly journals Intermediates of reversible photochemistry of phycoerythrocyanin α from Mastigocladus laminosus probed by low temperature absorption and circular dichroism spectroscopy

1999 ◽  
Vol 1 (1) ◽  
pp. 25-30 ◽  
Author(s):  
Kai-Hong Zhao ◽  
Hugo Scheer
Keyword(s):  
Circular Dichroism ◽  
Low Temperature ◽  
Circular Dichroism Spectroscopy ◽  
Spectral Changes ◽  
Mastigocladus Laminosus ◽  
Circular Dichroïsm

The reversible photochemistry of theα-subunit of phycoerythrocyanin (α-PEC) has been measured by low temperature absorption and circular dichroism in the range of 125K to 295 K. Below 185 K, the photochemistry is nearly silent; above 205 K, the photochemistry increases gradually without an indication of intermediates, and between 185 to 205K spectral changes in absorption and circular dichroism indicate an intermediate and/or changes in the interaction(s) between the chromophore and its environment.

Morphology and ultrastructure of the cyanobacterium Mastigocladus laminosus growing under nitrogen-fixing conditions

1984 ◽  
Vol 137 (2) ◽  
pp. 97-103 ◽  
Author(s):  
S. A. Nierzwicki-Bauer ◽  
D. L. Balkwill ◽  
S. E. Stevens
Keyword(s):  
Nitrogen Fixing ◽  
Mastigocladus Laminosus

scholarly journals Chromophore Assignment in C-Phycocyanin from Mastigocladus laminosus

1987 ◽  
Vol 42 (3) ◽  
pp. 258-262 ◽  
Author(s):  
S. Siebzehnrübl ◽  
R. Fischer ◽  
H. Scheer
Keyword(s):  
Circular Dichroism ◽  
Binding Sites ◽  
Specific Binding ◽  
Reactive Site ◽  
Spectral Changes ◽  
Mastigocladus Laminosus ◽  
Specific Binding Sites ◽  
Close Proximity ◽  
Circular Dichroïsm ◽  
Unambiguous Assignment

C-phycocyanin from the cyanobacterium, Mastigocladus laminosus, and its subunits have been treated with ρ-chloromercuribenzenesulfonate (PCMS). A single reactive site was found on the 13- subunit, and assigned to the single free cystein-β109. The concomitant spectral changes (absorp­tion, fluorescence, circular dichroism), together with the known close proximity of cys-β109 to chromophore β82, allowed an unambiguous assignment of the three spectrally, biochemically and functionally different chromophores to specific binding sites on the two peptide chains (α84: 616-618, β82: 622-624, β153: 598-600 nm).

Effect of Acetylene and Carbon Monoxide on Hydrogen Uptake and Evolution by Nitrogen-Starved Cultures of Mastigocladus laminosus

1981 ◽  
Vol 22 (8) ◽  
pp. 1375-1383 ◽  
Author(s):  
Yoshiharu Miura ◽  
Hiroaki Yokoyama ◽  
Motohiko Kimura ◽  
Tsuneko Iwamoto ◽  
Kazuhisa Miyamoto
Keyword(s):  
Carbon Monoxide ◽  
Hydrogen Uptake ◽  
Mastigocladus Laminosus
Sign in / Sign up

Export Citation Format

Share Document