PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15147208-5 2004 The proximal pocket of leghemoglobin is designed to favor strong coordination bonds between the heme iron and axial ligands. Heme 96-100 leghemoglobin A Glycine max 23-36 12486718-0 2003 Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin. Heme 7-11 leghemoglobin A Glycine max 73-86 12486718-9 2003 Thus, the leghemoglobin distal heme pocket provides a much lower barrier to oxygen association than occurs in myoglobin and oxygen dissociation is regulated from the proximal heme pocket. Heme 31-35 leghemoglobin A Glycine max 10-23 12486718-9 2003 Thus, the leghemoglobin distal heme pocket provides a much lower barrier to oxygen association than occurs in myoglobin and oxygen dissociation is regulated from the proximal heme pocket. Heme 175-179 leghemoglobin A Glycine max 10-23 11835502-0 2002 The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme. Heme 27-31 leghemoglobin A Glycine max 4-17 11835502-0 2002 The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme. Heme 88-92 leghemoglobin A Glycine max 4-17 11835502-2 2002 Lba has a much higher affinity for most ligands, and the two proteins use different distal and proximal heme pocket regulatory mechanisms to control ligand binding. Heme 104-108 leghemoglobin A Glycine max 0-3 10958321-5 2000 On the contrary, in leghemoglobin-a no spectral splitting upon nicotinate binding is observed, pointing to a planar heme configuration in which only distortions of A(1g)-type symmetry are effective and to which the nicotinate ring is bound in an x - y symmetric position. Heme 116-120 leghemoglobin A Glycine max 20-35 10958321-7 2000 Leghemoglobin-a behaves as a softer matrix with respect to horse myoglobin, thus validating the hypothesis of a looser heme pocket conformation in the former protein, which allows a nondistorted heme configuration and a symmetric binding of the bulky nicotinate ligand. Heme 119-123 leghemoglobin A Glycine max 0-15 10958321-7 2000 Leghemoglobin-a behaves as a softer matrix with respect to horse myoglobin, thus validating the hypothesis of a looser heme pocket conformation in the former protein, which allows a nondistorted heme configuration and a symmetric binding of the bulky nicotinate ligand. Heme 195-199 leghemoglobin A Glycine max 0-15 9536042-0 1998 Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules Although it is well established that the plant host encodes and synthesizes the apoprotein for leghemoglobin in root nodules, the source of the heme moiety has been uncertain. Heme 45-49 leghemoglobin A Glycine max 60-73 9536042-0 1998 Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules Although it is well established that the plant host encodes and synthesizes the apoprotein for leghemoglobin in root nodules, the source of the heme moiety has been uncertain. Heme 45-49 leghemoglobin A Glycine max 61-74 9536042-0 1998 Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules Although it is well established that the plant host encodes and synthesizes the apoprotein for leghemoglobin in root nodules, the source of the heme moiety has been uncertain. Heme 46-50 leghemoglobin A Glycine max 60-73 9536042-0 1998 Evidence that the plant host synthesizes the heme moiety of leghemoglobin in root nodules Although it is well established that the plant host encodes and synthesizes the apoprotein for leghemoglobin in root nodules, the source of the heme moiety has been uncertain. Heme 46-50 leghemoglobin A Glycine max 61-74 9536042-5 1998 Because these are the same cells that express apoleghemoglobin, the data strongly support a role for the plant in the synthesis of the heme moiety of leghemoglobin. Heme 136-140 leghemoglobin A Glycine max 151-164 15299933-5 1997 The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding. Heme 123-127 leghemoglobin A Glycine max 84-97 15299933-5 1997 The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding. Heme 216-220 leghemoglobin A Glycine max 84-97 9086279-12 1997 All of these results support the hypothesis that the high affinity of Lba for oxygen and other ligands is determined primarily by enhanced accessibility and reactivity of the heme group. Heme 175-179 leghemoglobin A Glycine max 70-73 2246244-3 1990 X-ray crystallography has shown that the heme cavity can easily accommodate ligands the size of nicotinate, and analysis of extended x-ray absorption fine structure data has shown that the Fe atom is in the mean plane of the heme in the leghemoglobin-CO complex. Heme 41-45 leghemoglobin A Glycine max 237-250 2246244-3 1990 X-ray crystallography has shown that the heme cavity can easily accommodate ligands the size of nicotinate, and analysis of extended x-ray absorption fine structure data has shown that the Fe atom is in the mean plane of the heme in the leghemoglobin-CO complex. Heme 225-229 leghemoglobin A Glycine max 237-250 3479799-0 1987 Bacterial heme synthesis is required for expression of the leghemoglobin holoprotein but not the apoprotein in soybean root nodules. Heme 10-14 leghemoglobin A Glycine max 59-72 3479799-1 1987 In Bradyrhizobium japonicum/soybean symbiosis, the leghemoglobin (legume hemoglobin) apoprotein is a plant product, but the origin of the heme prosthetic group is not known. Heme 138-142 leghemoglobin A Glycine max 51-64 3479799-5 1987 Data show that bacterial heme synthesis is required for leghemoglobin expression, but the heme moiety is not essential for apoleghemoglobin synthesis by the plant. Heme 25-29 leghemoglobin A Glycine max 56-69 3013619-0 1986 Heme regulates the expression in Saccharomyces cerevisiae of chimaeric genes containing 5"-flanking soybean leghemoglobin sequences. Heme 0-4 leghemoglobin A Glycine max 108-121 3706726-4 1986 Unexpected heme containing proteins eluted just after leghemoglobin a and the c complex. Heme 11-15 leghemoglobin A Glycine max 54-67 16593670-1 1986 Previous studies of legume nodules have indicated that formation of the heme moiety of leghemoglobin is a function of the bacterial symbiont. Heme 72-76 leghemoglobin A Glycine max 87-100 4040516-7 1985 The migration from the solvent to the heme pocket is much faster in Lb than in Mb. Heme 38-42 leghemoglobin A Glycine max 68-70 6682101-0 1983 Proton nuclear magnetic resonance study of the dynamic stability of the heme pocket of soybean leghemoglobin a. Heme 72-76 leghemoglobin A Glycine max 95-108 6682101-9 1983 Comparison between the same form of leghemoglobin and myoglobin reveals that the former exhibits exchange rates an order of magnitude faster than the latter protein in both ligated and unligated states, confirming the greater flexibility of the heme pocket in leghemoglobin. Heme 245-249 leghemoglobin A Glycine max 36-49 6682101-9 1983 Comparison between the same form of leghemoglobin and myoglobin reveals that the former exhibits exchange rates an order of magnitude faster than the latter protein in both ligated and unligated states, confirming the greater flexibility of the heme pocket in leghemoglobin. Heme 245-249 leghemoglobin A Glycine max 260-273 7197933-0 1981 Comparison of the heme electronic and molecular structure of soybean leghemoglobin and sperm whale myoglobin by proton NMR. Heme 18-22 leghemoglobin A Glycine max 69-82 7194110-0 1981 Measurement of heme accessibility in soybean ferric leghemoglobin a and its complexes by proton magnetic relaxation. Heme 15-19 leghemoglobin A Glycine max 52-65 7191255-0 1980 Resonance Raman evidence for constrained heme structure in soybean leghemoglobin and its derivatives. Heme 41-45 leghemoglobin A Glycine max 67-80 7193485-1 1980 13C NMR of labelled alkyl isocyanide ligands has been used with a view to probe the protein environment around the heme site of Soybean leghemoglobin, and comparatively, those of sperm whale myoglobin and monomeric Glycera hemoglobin. Heme 115-119 leghemoglobin A Glycine max 136-149 7193485-6 1980 The results are interpreted as arising from a diminished steric hindrance to isocyanide binding with leghemoglobin, in conformity with the recently published X-ray structure which reports the existence of a large heme pocket on the distal side. Heme 213-217 leghemoglobin A Glycine max 101-114 656461-0 1978 Heme sulfuric anhydrides as soybean leghemoglobin structure probes. Heme 0-4 leghemoglobin A Glycine max 36-49 656461-4 1978 The visible spectrum of anhydride leghemoglobin is that of low spin heme. Heme 68-72 leghemoglobin A Glycine max 34-47 656461-5 1978 This suggests that anhydride leghemoglobin has a conformation with a covalent attachment via propionic acid side chain to lysine-57 and the sixth coordination position of the heme iron occupied by the distal histidine at position 61. Heme 175-179 leghemoglobin A Glycine max 29-42 16660108-1 1977 On the Role of Bacteroid delta-Aminolevulinic Acid Synthase and delta-Aminolevulinic Acid Dehydrase in the Synthesis of the Heme of Leghemoglobin. Heme 124-128 leghemoglobin A Glycine max 132-145 16660108-8 1977 Plant ALAD activity falls during development of both types of root nodules.These results support the contention that it is the bacteroid ALAS and ALAD activities, not those of the plant, that are directly involved in formation of leghemoglobin heme, suggesting that the bacteroid may be solely responsible for formation of leghemoglobin heme in the nodule symbiosis. Heme 244-248 leghemoglobin A Glycine max 230-243 16660108-8 1977 Plant ALAD activity falls during development of both types of root nodules.These results support the contention that it is the bacteroid ALAS and ALAD activities, not those of the plant, that are directly involved in formation of leghemoglobin heme, suggesting that the bacteroid may be solely responsible for formation of leghemoglobin heme in the nodule symbiosis. Heme 244-248 leghemoglobin A Glycine max 323-336 16660108-8 1977 Plant ALAD activity falls during development of both types of root nodules.These results support the contention that it is the bacteroid ALAS and ALAD activities, not those of the plant, that are directly involved in formation of leghemoglobin heme, suggesting that the bacteroid may be solely responsible for formation of leghemoglobin heme in the nodule symbiosis. Heme 337-341 leghemoglobin A Glycine max 230-243 184092-2 1976 Electron paramagnetic resonance (EPR) and optical spectra are used as probes of the heme and its ligands in ferric and ferrous leghemoglobin. Heme 84-88 leghemoglobin A Glycine max 127-140 184092-3 1976 The proximal ligand to the heme iron atom of ferric soybean leghemoglobin is identified as imidazole by comparison of the EPR of leghemoglobin hydroxide, azide, and cyanide with the corresponding derivatives of human hemoglobin. Heme 27-31 leghemoglobin A Glycine max 60-73 184092-3 1976 The proximal ligand to the heme iron atom of ferric soybean leghemoglobin is identified as imidazole by comparison of the EPR of leghemoglobin hydroxide, azide, and cyanide with the corresponding derivatives of human hemoglobin. Heme 27-31 leghemoglobin A Glycine max 129-142 1238108-2 1975 Circular dichroism spectra in the far-ultraviolet show that the leghemoglobins all have a high alpha-helix content (soybean leghemoglobin a, 55%) regardless of the nature of bound ligands and oxidation or spin state of the heme iron. Heme 223-227 leghemoglobin A Glycine max 64-77 1238108-12 1975 The aromatic Soret and visible circular dichroism spectra for all derivatives of leghemoglobin are opposite in sense to those for myoglobin, showing that the patterns of protein side chain contacts with the heme are different in the two classes of heme proteins. Heme 207-211 leghemoglobin A Glycine max 81-94 1238108-12 1975 The aromatic Soret and visible circular dichroism spectra for all derivatives of leghemoglobin are opposite in sense to those for myoglobin, showing that the patterns of protein side chain contacts with the heme are different in the two classes of heme proteins. Heme 248-252 leghemoglobin A Glycine max 81-94 16656457-1 1966 When soybean nodules are incubated with propionate-2-(14)C the heme moiety of leghemoglobin becomes labeled. Heme 63-67 leghemoglobin A Glycine max 78-91 22308405-7 2012 In vitro nitration of Lba with excess nitrite produced several isomers of nitrated heme, one of which is identical to those found in vivo. Heme 83-87 leghemoglobin A Glycine max 22-25