PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29621505-0	2018	Structure of the NDH-2 - HQNO inhibited complex provides molecular insight into quinone-binding site inhibitors.	quinone	80-87	NADH-ubiquinone reductase (H(+)-translocating) NDE2	Saccharomyces cerevisiae S288C	17-22	
16884501-2	2006	Type II NADH dehydrogenases (NDH-2) are monomeric enzymes that catalyse quinone reduction and allow electrons to enter the respiratory chain in different organisms including higher plant mitochondria, bacteria and yeasts.	quinone	72-79	NADH-ubiquinone reductase (H(+)-translocating) NDE2	Saccharomyces cerevisiae S288C	29-34	
29621505-5	2018	The interaction of HQNO with bacterial NDH-2 is very similar to the native substrate ubiquinone (UQ1) interactions in the yeast Ndi1-UQ1 complex structure, suggesting a conserved mechanism for quinone binding.	quinone	88-95	NADH-ubiquinone reductase (H(+)-translocating) NDE2	Saccharomyces cerevisiae S288C	39-44	
24444429-6	2014	Comparison of bacterial NDH-2 with the yeast NADH dehydrogenase (Ndi1) structure revealed non-overlapping binding sites for quinone and NADH in the bacterial enzyme.	quinone	124-131	NADH-ubiquinone reductase (H(+)-translocating) NDE2	Saccharomyces cerevisiae S288C	24-29	
22949654-2	2012	In various organisms, complex I can be replaced by the alternative NADH-quinone oxidoreductase (NDH-2), which catalyzes the transfer of an electron from NADH via FAD to quinone, without proton pumping.	quinone	72-79	NADH-ubiquinone reductase (H(+)-translocating) NDE2	Saccharomyces cerevisiae S288C	96-101