PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2835176-5	1987	In mutant devoid of core protein I, cytochrome b was found to be reducible by NADH but not by succinate, suggesting two different electron transfer pathways inside comples III from each substrate to cytochrome b heme(s).	NAD	78-82	cytochrome b	Saccharomyces cerevisiae S288C	36-48	
6274398-2	1981	The doses required for 50% inhibition were 0.58 mol myxothiazol/mol cytochrome b for oxygen consumption of beef heart mitochondria, and 0.45 mol/mol cytochrome b for NADH oxidation by submitochondrial particles.	NAD	166-170	cytochrome b	Saccharomyces cerevisiae S288C	149-161	
6086348-14	1984	Comparing electron flow rates of succinate:cytochrome c oxidoreductase and NADH:cytochrome c oxidoreductase in cob- mutants and two revertants provides evidence that ubiquinone does not constitute a homogeneous pool, suggested by the dissimilar interaction of both dehydrogenases with the bc1 segment.	NAD	75-79	cytochrome b	Saccharomyces cerevisiae S288C	111-114	
6698026-12	1984	A cytochrome of type b with an absorption maximum at 559 nm accumulates during starvation only in queuine-lacking cells; it might be a component of an NAD-independent lactic acid oxidoreductase as is cytochrome b 557 in yeast and be responsible for the reduced level of lactate in cells lacking queuine in tRNA.	NAD	151-154	cytochrome b	Saccharomyces cerevisiae S288C	200-212