The interaction of leghemoglobin with nitrogen and with xenon.
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Chemical Phenomena↗
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Leghemoglobin: the role of hemoglobin in the nitrogen-fixing legume root nodule.
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Animals↗
Comparisons of nitrogen fixation estimates in soybeans by nodule weight, leghemoglobin content, and acetylene reduction.
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Acetylene↗
Leghemoglobin: sequence of amino acids around the two histidyl residues--a correction.
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Amino Acid Sequence↗
Crystalline leghemoglobin. 13. Sedimentation studies.
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Buffers↗
The primary structure of soybean leghemoglobin.
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Amino Acid Sequence↗
The primary structure of soybean leghemoglobin. I. The separation of the tryptic peptides of the apoprotein from the slow component and their amino acid compositions.
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Amino Acids↗
The primary structure of soybean leghemoglobin. II. Amino acid sequence of seventeen peptides isolated from the tryptic hydrolysate of the slow component.
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Amino Acid Sequence↗
Crystalline leghemoglobin. XIV. Transfer of hematin from Lba and Lbc to horse-radish peroxidase apoprotein.
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Apoproteins↗
The primary structure of soybean leghemoglobin. 3. Fractionation and sequence of chymotryptic peptides of the apoprotein of the slow component.
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Amino Acid Sequence↗
The primary structure of soybean leghemoglobin. IV. Fractionation and sequence of thermolytic peptides of the apoprotein of the slow component (Lba).
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Amino Acid Sequence↗
Purification and properties of Phaseolus vulgaris leghemoglobin (PhLb).
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Amino Acids↗
The kinetics of the reactions of leghemoglobin with oxygen and carbon monoxide.
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Acetates↗
Leghemoglobin. I. Changes in conformation and chemical reactivity linked to reaction with acetic acid.
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Acetates↗
Leghemoglobin. II. Changes in conformation and chemical reactivity linked to reaction with a dissociable low molecular weight ligand, X.
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Binding Sites↗
Facilitated oxygen diffusion. The role of leghemoglobin in nitrogen fixation by bacteroids isolated from soybean root nodules.
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Acetylene↗
Equilibria and kinetics of ligand binding by leghemoglobin from soybean root nodules.
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Carbon Monoxide↗
Peroxidase content of soybean root nodules.
A peroxidase has been isolated from soybean nodules and its main characteristics have been determined. Its molecular weight (48 000) and spectral properties are similar to those of usual plant peroxidases. Its activity is comparable to that of low-efficiency plant peroxidases. The rate constant of the reaction with H2O2 is 3 x 10(5) M-1 x s-1. In this reaction, nodule peroxidase yields an oxidized intermediate analogous to the compound I species of peroxidases already studied. A comparison is made with the pseudoperoxidatic activity of soybean leghemoglobin components. Leghemoglobins a and c react with H2O2 with rate constants of 5 x 10(3) and 2.5 x 10(3) M-1 x s-1, respectively, yielding the leghemoglobin (IV) species. During these reactions leghemoglobins are inactivated.
Kinetics↗