Characterization of purified c-type heme-containing peptides and identification of c-type heme-attachment sites in Shewanella oneidenis cytochromes using mass spectrometry |
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Authors: | Yang Feng Bogdanov Bogdan Strittmatter Eric F Vilkov Andrey N Gritsenko Marina Shi Liang Elias Dwayne A Ni Shuisong Romine Margaret Pasa-Tolić Ljiljana Lipton Mary S Smith Richard D |
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Institution: | Biological Sciences Division and Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, P.O. Box 999, Richland, Washington 99352, USA. |
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Abstract: | We describe methods for mass spectrometric identification of heme-containing peptides from c-type cytochromes that contain the CXXCH (X=any amino acid) sequence motif. The heme fragment ion yielded the most abundant MS/MS peak for standard heme-containing peptides with one amino acid difference for both 2+ and 3+ peptide charge states; both sequence and charge affect the extent of heme loss. Application to Shewanella oneidenis demonstrated the utility of this approach for identifying c-type heme-containing peptides from complex proteome samples. |
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