Isolation and characterization of a novel membrane-bound cytochrome c553 from the strictly anaerobic phototroph, Heliobacillus mobilis

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Title
Isolation and characterization of a novel membrane-bound cytochrome c553 from the strictly anaerobic phototroph, Heliobacillus mobilis
Author(s)
Woo-Yiel Lee; R E Blankenship; Seung Ho Kim
Bibliographic Citation
Journal of Microbiology, vol. 35, no. 3, pp. 206-212
Publication Year
1997
Abstract
Heliobacillus mobilis is a strictly anaerobic Gram-positive bacterium which contains a primitive Photosystem I-type reaction center. The membrane-bound cytochrome c553 from the heliobacterium suggested to be the immediate electron donor to the photooxidized pigment (P 798+) has been isolated and characterized. The heme protein was visualized as a major component with an apparent molecular size of 17 kDa in TMBZ-staining analysis of the membrane preparation and showed characteristic α (552.5 nm), β (522 nm), and Soret absorption (416 nm) peaks of a typical reduced c-type cytochrome in the partially purified sample. The internal 43 amino acid sequence of the electron donor was obtained by chemical agent and protease treatments followed by N-terminal sequencing of the resulting fragments. The internal sequence carries lots of lysine residues and a Cys-X-X-Cys-His sequence motif which are the characteristics of typical c-type cytochromes. The analysis of the sequence by FAST or FASTA program, however, did not show any significant similarity to other known heme proteins.
Keyword
Isolationcharacterizationnovel membrane-bound c-type cytochromesecondary electron donorheliobacteria
ISSN
1225-8873
Publisher
Microbiological Society Korea
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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