PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
16928691-3	2006	To investigate the electron transfer pathway from CPR to HO, we examined the reactions of heme and verdoheme, the second intermediate in the heme degradation, complexed with rat HO-1 (rHO-1) using a rat FMN-depleted CPR; the FMN-depleted CPR was prepared by dialyzing the CPR mutant, Y140A/Y178A, against 2 m KBr.	verdoheme	99-108	cytochrome p450 oxidoreductase	Rattus norvegicus	50-53
18778686-9	2008	Consequently, in the physiological oxygen reactions, the verdoheme is found to be stabilized in the ferric state in GmHO-1 probably guided by protein distal residues and in the ferrous state in rHO-1, whereas in the hydrogen peroxide reactions, hydrogen peroxide or hydroxide coordination stabilizes the ferric state of verdoheme in both HOs.	verdoheme	57-66	heme oxygenase 1	Rattus norvegicus	194-199
19694439-10	2009	Much tighter binding of the inhibitor to the verdoheme intermediate differentiates it from inhibition of, for example, CYP3A4 and offers a possible route to more selective inhibitor design.	verdoheme	45-54	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	119-125
17253780-9	2007	Furthermore, the biochemical characterization revealed that the catalytic reactions of both HO-1 and HO-2 were completely stopped after the formation of verdoheme in the presence of the imidazole-dioxolane compound.	verdoheme	153-162	heme oxygenase 1	Rattus norvegicus	92-105
16928691-3	2006	To investigate the electron transfer pathway from CPR to HO, we examined the reactions of heme and verdoheme, the second intermediate in the heme degradation, complexed with rat HO-1 (rHO-1) using a rat FMN-depleted CPR; the FMN-depleted CPR was prepared by dialyzing the CPR mutant, Y140A/Y178A, against 2 m KBr.	verdoheme	99-108	heme oxygenase 1	Rattus norvegicus	178-182
16928691-3	2006	To investigate the electron transfer pathway from CPR to HO, we examined the reactions of heme and verdoheme, the second intermediate in the heme degradation, complexed with rat HO-1 (rHO-1) using a rat FMN-depleted CPR; the FMN-depleted CPR was prepared by dialyzing the CPR mutant, Y140A/Y178A, against 2 m KBr.	verdoheme	99-108	heme oxygenase 1	Rattus norvegicus	184-189
16928691-6	2006	In contrast, verdoheme was converted to the ferric biliverdin-iron chelate with FMN-depleted CPR, and this conversion was inhibited by ferricyanide, indicating that electrons are certainly required for conversion of verdoheme to a ferric biliverdin-iron chelate and that they can be supplied from the FMN-depleted CPR through a pathway not involving FMN, probably via FAD.	verdoheme	13-22	cytochrome p450 oxidoreductase	Rattus norvegicus	93-96
16928691-6	2006	In contrast, verdoheme was converted to the ferric biliverdin-iron chelate with FMN-depleted CPR, and this conversion was inhibited by ferricyanide, indicating that electrons are certainly required for conversion of verdoheme to a ferric biliverdin-iron chelate and that they can be supplied from the FMN-depleted CPR through a pathway not involving FMN, probably via FAD.	verdoheme	13-22	cytochrome p450 oxidoreductase	Rattus norvegicus	314-317
16928691-6	2006	In contrast, verdoheme was converted to the ferric biliverdin-iron chelate with FMN-depleted CPR, and this conversion was inhibited by ferricyanide, indicating that electrons are certainly required for conversion of verdoheme to a ferric biliverdin-iron chelate and that they can be supplied from the FMN-depleted CPR through a pathway not involving FMN, probably via FAD.	verdoheme	216-225	cytochrome p450 oxidoreductase	Rattus norvegicus	314-317
10373419-1	1999	Whether or not reducing equivalents are indispensable for the conversion of ferric alpha-hydroxyheme bound to heme oxygenase-1 to verdoheme remains controversial (Matera, K. M., Takahashi, S., Fujii, H., Zhou, H., Ishikawa, K., Yoshimura, T., Rousseau, D. L., Yoshida, T., and Ikeda-Saito, M. (1996) J. Biol.	verdoheme	130-139	heme oxygenase 1	Homo sapiens	110-126
15606196-6	2004	Exposure of the one-electron- or two-electron-reduced verdoheme complexes of cytochrome b(5) to O(2) results in rapid and quantitative reoxidation to the resting state [Fe(II)(verdoheme)](+) complex.	verdoheme	54-63	mitochondrially encoded cytochrome b	Homo sapiens	77-89
15606196-6	2004	Exposure of the one-electron- or two-electron-reduced verdoheme complexes of cytochrome b(5) to O(2) results in rapid and quantitative reoxidation to the resting state [Fe(II)(verdoheme)](+) complex.	verdoheme	176-185	mitochondrially encoded cytochrome b	Homo sapiens	77-89
12809497-5	2003	Heme oxygenase-1 converted all four isomers of meso-hydroxyhemin to the corresponding isomers of verdoheme.	verdoheme	97-106	heme oxygenase 1	Rattus norvegicus	0-16
10373419-11	1999	The verdoheme formed from alpha-hydroxyheme was shown to be in the ferrous oxidation state by the addition of CO or potassium ferricyanide to the resultant verdoheme-heme oxygenase-1 complex.	verdoheme	4-13	heme oxygenase 1	Homo sapiens	166-182
7890772-7	1995	The reaction with hydrogen peroxide converted the heme of the heme oxygenase-2 fragment complex into a verdoheme-like intermediate, while the reaction with m-chloroperbenzoic acid yielded a oxoferryl species.	verdoheme	103-112	heme oxygenase 2	Homo sapiens	62-78