PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17349966-9	2007	A modified path for proton uptake towards the Q(i)-site features a cluster of conserved lysine residues in the cytochrome b (Lys228) and cytochrome c(1) subunits (Lys288, Lys289, Lys296).	Lysine	88-94	cytochrome b	Saccharomyces cerevisiae S288C	111-123	
2557894-2	1989	A different residue, which is most likely lysine, is the sixth heme ligand in oxidized spinach cytochrome f. The data for oxidized yeast cytochrome b are consistent with bis-histidine coordination of both hemes although the possibility that one of the hemes is ligated by histidine and lysine cannot be rigorously excluded.	Lysine	42-48	cytochrome b	Saccharomyces cerevisiae S288C	137-149	
10216163-3	1999	We identify Lys-132 in the Sdh4p C-terminal region as necessary for enzyme stability, ubiquinone reduction, and cytochrome b562 assembly in SDH.	Lysine	12-15	cytochrome b	Saccharomyces cerevisiae S288C	112-124