PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33436601-4	2021	One of the confined enzymes, ferredoxin-NADP+ reductase, serves as a transducer, rapidly and reversibly recycling nicotinamide cofactors electrochemically for immediate delivery to the next enzyme along the chain, thereby making it possible to energize, control and observe extended cascade reactions driven in either direction depending on the electrode potential that is applied.	Niacinamide	114-126	ferredoxin reductase	Homo sapiens	29-55	
22542899-9	2012	The overall findings indicate that in FNR the volume of the residue at position 266 is essential to attain the catalytic architecture between the nicotinamide and isoalloxazine rings at the active site and, therefore, for an efficient HT process.	Niacinamide	146-158	ferredoxin reductase	Homo sapiens	38-41	
16216071-2	2005	During hydride transfer it is proposed that the FNR C-terminal Tyr is displaced by the nicotinamide.	Niacinamide	87-99	ferredoxin reductase	Homo sapiens	48-51	
7677850-1	1995	The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H).	Niacinamide	167-179	ferredoxin reductase	Homo sapiens	25-51	
21538059-5	2012	In particular, the side chain of the C-terminal Y303 in Anabaena FNR appears key to providing the optimum geometry by reducing the stacking probability between the isoalloxazine and nicotinamide rings, thus providing the required co-linearity and distance among the N5 of the flavin cofactor, the C4 of the coenzyme nicotinamide and the hydride that has to be transferred between them.	Niacinamide	182-194	ferredoxin reductase	Homo sapiens	65-68	
21538059-5	2012	In particular, the side chain of the C-terminal Y303 in Anabaena FNR appears key to providing the optimum geometry by reducing the stacking probability between the isoalloxazine and nicotinamide rings, thus providing the required co-linearity and distance among the N5 of the flavin cofactor, the C4 of the coenzyme nicotinamide and the hydride that has to be transferred between them.	Niacinamide	316-328	ferredoxin reductase	Homo sapiens	65-68	
20471952-7	2010	The architecture of the WT FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient HT processes.	Niacinamide	130-142	ferredoxin reductase	Homo sapiens	27-30	
20471952-7	2010	The architecture of the WT FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient HT processes.	Niacinamide	290-302	ferredoxin reductase	Homo sapiens	27-30	
10744737-0	2000	Competition between C-terminal tyrosine and nicotinamide modulates pyridine nucleotide affinity and specificity in plant ferredoxin-NADP(+) reductase.	Niacinamide	44-56	ferredoxin reductase	Homo sapiens	121-149	
7677850-1	1995	The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H).	Niacinamide	167-179	ferredoxin reductase	Homo sapiens	53-56	
7677850-6	1995	However, spectral perturbations induced by NADP+ binding to FNR-S96V strongly resemble those elicited by the binding of 2"-monophosphoadenosine-5"-diphosphoribose, a substrate analog lacking the nicotinamide ring, both to the mutant and wild-type enzymes.	Niacinamide	195-207	ferredoxin reductase	Homo sapiens	60-63	
3394171-6	1988	These data support the conclusion about the existence of second nicotinamide coenzyme binding centre in adrenodoxin reductase.	Niacinamide	64-76	ferredoxin reductase	Homo sapiens	104-125