PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3136803-1	1988	The iron coordination in native, Fe(II), lipoxygenase has been studied by Extended X-Ray Absorption Fine Structure (EXAFS).	Iron	4-8	linoleate 9S-lipoxygenase-4	Glycine max	33-53	
186306-0	1976	On the interaction of some catechol derivatives with the iron atom of soybean lipoxygenase.	Iron	57-61	linoleate 9S-lipoxygenase-4	Glycine max	78-90	
3040731-2	1987	Soybean lipoxygenase is a non-heme iron enzyme that catalyzes the hydroperoxidation of linoleic acid by dioxygen.	Iron	35-39	linoleate 9S-lipoxygenase-4	Glycine max	8-20	
16665148-6	1986	The incorporation of iron-59 from the nutrient medium into lipoxygenase during culture of immature seeds was indicative of de novo synthesis of the enzyme.	Iron	21-25	linoleate 9S-lipoxygenase-4	Glycine max	59-71	
16665148-7	1986	The efficiency of the iron uptake was high, as indicated by the level of radioactivity found in the enzyme (one gram atom of iron per mole of lipoxygenase).	Iron	22-26	linoleate 9S-lipoxygenase-4	Glycine max	142-154	
16665148-7	1986	The efficiency of the iron uptake was high, as indicated by the level of radioactivity found in the enzyme (one gram atom of iron per mole of lipoxygenase).	Iron	125-129	linoleate 9S-lipoxygenase-4	Glycine max	142-154	
6776357-9	1980	With iron-supplemented microsomes from rat liver, the compounds formed were qualitatively and quantitatively the same as with soybean lipoxygenase, whereas with 18,000 X g rat liver supernatant fractions the yields of all products formed--except 7 alpha-hydroxycholesterol and 6 beta-hydroxy-4-cholesten-3-one--were markedly decreased.	Iron	5-9	linoleate 9S-lipoxygenase-4	Glycine max	134-146	
24767084-5	2014	The allosteric (or cooperative) inhibition of soybean lipoxygenase-1 of longer alkyl protocatechuates is reversible but in combination with their iron binding ability to disrupt the active site competitively and to interact with the hydrophobic portion surrounding near the active site (sequential action).	Iron	146-150	linoleate 9S-lipoxygenase-4	Glycine max	54-66	
27532889-0	2016	Computational Insights into Five- versus Six-Coordinate Iron Center in Ferrous Soybean Lipoxygenase.	Iron	56-60	linoleate 9S-lipoxygenase-4	Glycine max	87-99	
11412104-3	2001	This study utilizes a combination of kinetic and structural probes to relate the lipoxygenase mechanism of action with structural modifications of the iron"s second coordination sphere.	Iron	151-155	linoleate 9S-lipoxygenase-4	Glycine max	81-93	
18067328-4	2008	Controlling the redox state of lipoxygenase iron with small molecules, inhibitors or activators, could be a means to modulate the activity of the enzyme.	Iron	44-48	linoleate 9S-lipoxygenase-4	Glycine max	31-43	
18067328-10	2008	Oxidation of the iron in lipoxygenase-1 by 2-hydroperoxyalkanes was evident in electron paramagnetic resonance (EPR) measurements, but the enzyme was neither activated nor was it inactivated.	Iron	17-21	linoleate 9S-lipoxygenase-4	Glycine max	25-37	
11602611-1	2001	The structural and physiochemical properties of 3-hydroxypyridin-4-one chelators (HPOs) which influence inhibition of the iron-containing metalloenzymes ribonucleotide reductase (RR) and 5-lipoxygenase (5-LO) have been investigated.	Iron	122-126	linoleate 9S-lipoxygenase-4	Glycine max	189-201	
7999760-4	1994	The coordination of the iron(II) in native lipoxygenase changes when methanol (as low as 0.1%) or glycerol (20%) is added to the buffer prior to freezing.	Iron	24-28	linoleate 9S-lipoxygenase-4	Glycine max	43-55	
9922163-6	1998	These observations reveal specific details of the interaction between lipoxygenase and a small molecule and raise the possibility that changes in the ligand environment of the iron atom could be a feature of the product activation reaction or the catalytic mechanism.	Iron	160-164	linoleate 9S-lipoxygenase-4	Glycine max	70-82	
7999760-9	1994	The iron coordination in iron(III) lipoxygenase is less affected by the presence of alcohols than is the site in the iron(II) enzyme.	Iron	4-8	linoleate 9S-lipoxygenase-4	Glycine max	35-47	
7999760-9	1994	The iron coordination in iron(III) lipoxygenase is less affected by the presence of alcohols than is the site in the iron(II) enzyme.	Iron	25-29	linoleate 9S-lipoxygenase-4	Glycine max	35-47	
8142401-5	1994	In reactions started with mixtures of iron(II) and iron(III) lipoxygenase, r(init) is linearly related to the initial concentration of the Fe (III) enzyme form.	Iron	38-42	linoleate 9S-lipoxygenase-4	Glycine max	61-73	
8188678-7	1994	Mutagenesis and deletion of the highly conserved lipoxygenase C-terminal isoleucine (Ile663), a residue believed to be involved in the non-heme iron atom coordination of all lipoxygenases, was performed.	Iron	144-148	linoleate 9S-lipoxygenase-4	Glycine max	49-61	
8188678-10	1994	These findings would tend to indicate a stringent requirement for the proper spatial alignment and folding of the C-terminal chain back into the core of the enzyme to interact with the iron atom by analogy with the recently determined crystal structure of a soybean lipoxygenase (Boyington, J. C., Gaffney, B. J., and Amzel, L. M. (1993) Science 260, 1482-1486).	Iron	185-189	linoleate 9S-lipoxygenase-4	Glycine max	266-278	
1850741-2	1991	Using soybean lipoxygenase-1 as a model, we have shown that two classes of lipoxygenase inhibitors currently in development as potential antiinflammatory agents obtain a significant amount of their potency by reducing the lipoxygenase active-site iron from the active ferric state to the inactive ferrous state.	Iron	247-251	linoleate 9S-lipoxygenase-4	Glycine max	14-26	
1850741-2	1991	Using soybean lipoxygenase-1 as a model, we have shown that two classes of lipoxygenase inhibitors currently in development as potential antiinflammatory agents obtain a significant amount of their potency by reducing the lipoxygenase active-site iron from the active ferric state to the inactive ferrous state.	Iron	247-251	linoleate 9S-lipoxygenase-4	Glycine max	75-87	
2164931-0	1990	The initial characterization of the iron environment in lipoxygenase by Mossbauer spectroscopy.	Iron	36-40	linoleate 9S-lipoxygenase-4	Glycine max	56-68	
2164931-1	1990	The incorporation of 57Fe into two lipoxygenase isoenzymes from soybeans has been achieved making possible the first observations of the iron environment in these proteins using Mossbauer spectroscopy.	Iron	137-141	linoleate 9S-lipoxygenase-4	Glycine max	35-47	
2164931-5	1990	Based on the sign of the electric field gradient, the most likely ligand sphere for the iron in native lipoxygenase consists of oxygen and nitrogen ligands in a roughly octahedral field of symmetry.	Iron	88-92	linoleate 9S-lipoxygenase-4	Glycine max	103-115	
2164931-9	1990	The Mossbauer spectra (4.2-250 K) for samples of both isoenzymes after oxidation of the iron in native enzyme by the product of lipoxygenase catalysis were extremely broad (20 mm/s) with no obvious narrow resonance lines.	Iron	88-92	linoleate 9S-lipoxygenase-4	Glycine max	128-140	
2164931-11	1990	A small molecule containing an iron site sharing many of these Mossbauer and electron paramagnetic resonance properties with lipoxygenase was identified: Fe(II)/(III).diethylenetriaminepentaacetic acid.	Iron	31-35	linoleate 9S-lipoxygenase-4	Glycine max	125-137