| Title | Isolation and characterization of a noval membrane-bound cytochrome C_553 from the strictly anaerobic phototroph, heliobacillus mobilis |
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| Author | Lee, Woo Yiel · Blankenship, Robert E.¹ · Kim, Seung Ho * |
| Address | Protein Function Research Uni, Korea Research Institute of Bioscience and biotechnology; ¹Department of Chemistry and Biochemistry, Arizona University |
| Bibliography | Journal of Microbiology, 35(3),206-212, 1997, |
| DOI | |
| Key Words | Isolation, characterization, novel membrane-bound c-type cytochrome, secondary electron donor, helicobacteria |
| Abstract | Heliobacillus mobilis is a strictly anaerobic Gram-positive bacterium which contains a primitive Photosystem I-type reaction center. The membrane-bound cytochrome c_553 from the heliobacterium suggested to be the immediate electron donor to the photooxidized pigment (P798+) has been isolated and characterized. The heme protein was visualized as a major component with an apparent molecular size of 17kDa in TMBZ-staining analysis of the membrane preparation and showed characteristic α (552.5 nm), β (522nm), 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. |
| Download PDF | Eng_350309_206-212p.pdf |