Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 11, Issue 10, Pages 1023-1024Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb827
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We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.
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