PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26211916-3 2015 While the 20-fold higher oxygen affinity of Lba compared with Mb is required for its dual physiological function, the mechanism by which this high affinity is achieved is only emerging. Oxygen 25-31 leghemoglobin A Glycine max 44-47 15147208-0 2004 Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin. Oxygen 65-71 leghemoglobin A Glycine max 83-96 15147208-6 2004 Thus, high oxygen affinity in leghemoglobin is established by a favorable staggered geometry of the proximal histidine. Oxygen 11-17 leghemoglobin A Glycine max 30-43 15147208-8 2004 If hydrogen bonding from His(E7) were as strong as it is in mammalian myoglobin, the resultant ultrahigh affinity of leghemoglobin would prevent oxygen transport in root nodules. Oxygen 145-151 leghemoglobin A Glycine max 117-130 12486718-2 2003 Leghemoglobin serves an additional role as an oxygen scavenger to prevent inhibition of nitrogen fixation. Oxygen 46-52 leghemoglobin A Glycine max 0-13 12486718-3 2003 For this purpose, the oxygen affinity of soybean leghemoglobin is 20-fold greater than myoglobin, resulting from an 8-fold faster association rate constant combined with a 3-fold slower dissociation rate constant. Oxygen 22-28 leghemoglobin A Glycine max 49-62 12486718-6 2003 Oxygen and carbon monoxide binding to a comprehensive set of leghemoglobin distal heme pocket mutant proteins in comparison to their myoglobin counterparts has revealed some of these mechanisms. Oxygen 0-6 leghemoglobin A Glycine max 61-74 12486718-8 2003 Furthermore, soybean leghemoglobin uses an unusual combination of HisE7 and TyrB10 to sustain a weak stabilizing interaction with bound oxygen. Oxygen 136-142 leghemoglobin A Glycine max 21-34 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. Oxygen 76-82 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. Oxygen 124-130 leghemoglobin A Glycine max 10-23 11835502-0 2002 The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme. Oxygen 47-53 leghemoglobin A Glycine max 4-17 11835502-3 2002 Removal of the constraint provided by covalent attachment of the proximal histidine to the F-helices of these proteins decreases oxygen affinity in Lba and increases oxygen affinity in Mb, mainly because of changes in oxygen dissociation rate constants. Oxygen 129-135 leghemoglobin A Glycine max 148-151 10647213-2 1999 Antioxidants are especially critical in root nodules because leghemoglobin, which is present at high concentrations in nodules, is prone to autoxidation and production of activated oxygen species such as O2.- and H2O2. Oxygen 181-187 leghemoglobin A Glycine max 61-74 10647213-2 1999 Antioxidants are especially critical in root nodules because leghemoglobin, which is present at high concentrations in nodules, is prone to autoxidation and production of activated oxygen species such as O2.- and H2O2. Oxygen 204-206 leghemoglobin A Glycine max 61-74 9086279-3 1997 Rate constants for O2, CO and NO binding to recombinant Lba are identical with those of native soybean Lba. Oxygen 19-21 leghemoglobin A Glycine max 56-59 9086279-9 1997 The His(E7) to Phe mutation does cause a significant decrease in K(O2) for Lba, apparently due to steric hindrance of the bound ligand. Oxygen 67-69 leghemoglobin A Glycine max 75-78 9086279-10 1997 The rate constants for O2 dissociation from wild-type and native Lba decrease significantly with decreasing pH. Oxygen 23-25 leghemoglobin A Glycine max 65-68 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. Oxygen 78-84 leghemoglobin A Glycine max 70-73 9201685-7 1997 The data and parameters presented are shown to serve as a basis for more extensive investigations of root nodules (e.g., the oxygen diffusion barrier or the mechanisms driving the regulation of the oxygen concentration in the infected zone by leghemoglobin) by NMR microimaging. Oxygen 198-204 leghemoglobin A Glycine max 243-256 8955081-2 1996 Reaction of H2O2 with ferric leghemoglobin (metLb, the monomeric, oxygen-carrying, heme protein from root nodules of nitrogen-fixing plants) has been previously shown to generate an iron(IV)-oxo (ferryl) species and at least one protein radical. Oxygen 66-72 leghemoglobin A Glycine max 29-42 12228427-3 1995 nodules during rapid and gradual changes in temperature from 20[deg]C to either 15 or 25[deg]C. The affinity of leghemoglobin for O2 was also measured at each temperature and the values were used to calculate the infected cell O2 concentration (Oi). Oxygen 130-132 leghemoglobin A Glycine max 112-125 8218216-0 1993 Role of hydrogen bonding to bound dioxygen in soybean leghemoglobin. Oxygen 34-42 leghemoglobin A Glycine max 54-67 8218216-7 1993 A discussion of the contribution of this hydrogen bond to the pH-dependent O2 affinity of leghemoglobin is presented. Oxygen 75-77 leghemoglobin A Glycine max 90-103 16652965-0 1992 Involvement of Molecular Oxygen in the Enzyme-Catalyzed NADH Oxidation and Ferric Leghemoglobin Reduction. Oxygen 25-31 leghemoglobin A Glycine max 82-95 2246244-0 1990 Kinetics and thermodynamics of oxygen, CO, and azide binding by the subcomponents of soybean leghemoglobin. Oxygen 31-37 leghemoglobin A Glycine max 93-106 2246244-1 1990 Leghemoglobin shows extreme high affinity behavior in the binding of both oxygen and CO. Oxygen 74-80 leghemoglobin A Glycine max 0-13 2246244-5 1990 At 20 degrees C the rate constants for oxygen and CO binding vary by 26-44% among the eight leghemoglobin components. Oxygen 39-45 leghemoglobin A Glycine max 92-105 2246244-10 1990 This finding calls into question models that ascribe a significant functional role to changes in the distribution of leghemoglobin components in regulating oxygen concentration in the nodule. Oxygen 156-162 leghemoglobin A Glycine max 117-130 34885789-1 2021 Leghemoglobin (Lb) is an oxygen-binding plant hemoglobin of legume nodules, which participates in the symbiotic nitrogen fixation process. Oxygen 25-31 leghemoglobin A Glycine max 0-13 24221924-6 1988 This is the first report of Lb in uninfected cells of any legume nodule; it raises the possibility that this important nodule-specific protein may participate in mediating oxygen flow to host plant organelles throughout the infected region of the nodule. Oxygen 172-178 leghemoglobin A Glycine max 28-30 4040516-0 1985 Dynamics of dioxygen and carbon monoxide binding to soybean leghemoglobin. Oxygen 12-20 leghemoglobin A Glycine max 60-73 4040516-1 1985 The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were investigated between 10 and 20 K. The general features of the binding process in leghemoglobin are similar to the ones found in myoglobin. Oxygen 19-27 leghemoglobin A Glycine max 59-72 4040516-1 1985 The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were investigated between 10 and 20 K. The general features of the binding process in leghemoglobin are similar to the ones found in myoglobin. Oxygen 19-27 leghemoglobin A Glycine max 74-76 4040516-1 1985 The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were investigated between 10 and 20 K. The general features of the binding process in leghemoglobin are similar to the ones found in myoglobin. Oxygen 19-27 leghemoglobin A Glycine max 332-345 6539095-5 1984 With ferric leghemoglobin (Lb) as the substrate, nearly identical initial velocities were obtained using either CO or O2 to ligate the enzymatically produced ferrous leghemoglobin. Oxygen 118-120 leghemoglobin A Glycine max 166-179 575296-8 1979 The increase in relative leghemoglobin a content suggests that leghemoglobin a might be required for regulation of nodule O2 concentration only when the nodule structure is complex. Oxygen 122-124 leghemoglobin A Glycine max 63-76