PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
34509493-0	2021	Human flavin-containing monooxygenase 1 and its long-sought hydroperoxyflavin intermediate.	hydroperoxyflavin	60-77	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	6-39
24321106-0	2013	C4a-hydroperoxyflavin formation in N-hydroxylating flavin monooxygenases is mediated by the 2"-OH of the nicotinamide ribose of NADP+.	hydroperoxyflavin	4-21	complement C4A (Rodgers blood group)	Homo sapiens	0-3
24321106-2	2013	Formation and decay of the C4a-hydroperoxyflavin were monitored under rapid reaction kinetic conditions in SidA, an N-hydroxylating monooxygenase involved in siderophore biosynthesis.	hydroperoxyflavin	31-48	complement C4A (Rodgers blood group)	Homo sapiens	27-30
18164311-4	2008	The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate.	hydroperoxyflavin	242-259	ladinin 1	Homo sapiens	4-8
18164311-4	2008	The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate.	hydroperoxyflavin	242-259	ladinin 1	Homo sapiens	44-48
12444653-8	2002	Classical energy barriers for oxygen atom transfer from neutral and ion-paired forms of C4a-hydroperoxyflavin to dimethyl sulfide are predicted to differ by a small margin, suggesting that proton distribution exerts a relatively small influence on the reactivity of alkyl hydroperoxides.	hydroperoxyflavin	92-109	complement C4A (Rodgers blood group)	Homo sapiens	88-91
26144862-4	2015	This complex undergoes intersystem crossing to form the open-shell singlet diradical complex before it forms the closed-shell singlet C4a-hydroperoxyflavin intermediate (C4aOOH).	hydroperoxyflavin	138-155	complement C4A (Rodgers blood group)	Homo sapiens	134-137
24878148-0	2014	Control of C4a-hydroperoxyflavin protonation in the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase.	hydroperoxyflavin	15-32	complement C4A (Rodgers blood group)	Homo sapiens	11-14
24368083-0	2014	Proton-coupled electron transfer and adduct configuration are important for C4a-hydroperoxyflavin formation and stabilization in a flavoenzyme.	hydroperoxyflavin	80-97	complement C4A (Rodgers blood group)	Homo sapiens	76-79
24368083-7	2014	Furthermore, the C4a-hydroperoxyflavin is stabilized by the side chains of Thr169, His548, and Asn593 in a "face-on" configuration where it can undergo a unimolecular reaction to generate H2O2 and oxidized flavin.	hydroperoxyflavin	21-38	complement C4A (Rodgers blood group)	Homo sapiens	17-20
21680741-0	2011	Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.	hydroperoxyflavin	21-38	complement C4A (Rodgers blood group)	Homo sapiens	17-20
21680741-0	2011	Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.	hydroperoxyflavin	21-38	complement C4A (Rodgers blood group)	Homo sapiens	139-142