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Journal ArticleDOI

The redox potential of leghaemoglobin.

R.W. Henderson, +1 more
- 13 Oct 1972 - 
- Vol. 283, Iss: 1, pp 187-191
TLDR
The results contradict an earlier reported suggestion that leghaemoglobin functions at low pH values as a vigorous electron donor capable of producing atomic hydrogen.
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This article is published in Biochimica et Biophysica Acta.The article was published on 1972-10-13. It has received 20 citations till now. The article focuses on the topics: Potentiometric titration & Redox.

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Citations
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Journal ArticleDOI

What are hemoglobins doing in plants

Robert D Hill
- 01 May 1998 - 
TL;DR: Some of the evidence to support the postulated view that hemoglobin acts as an oxygenase in plants is presented and some of the properties of a barley hemoglobin are described.
Journal ArticleDOI

CO and O2 complexes of soybean leghemoglobins: pH effects upon infrared and visible spectra. Comparisons with CO and O2 complexes of myoglobin and hemoglobin.

TL;DR: The data are consistent with a model in which protonation of the distal histidine permits protein-free heme FeCO geometry in leghemoglobin-- CO complexes but not in myoglobin-- or hemoglobin--CO complexes, and the heme pockets of leghemoglobins appear to be more flexible than the he me pockets of myoglobin and hemoglobin.
Book ChapterDOI

The oxidation states and reversible redox reactions of metalloporphyrins

TL;DR: In this paper, the metal-free Porphyr in bases, their prefixes and suffixes and their exponentiations are given. But they do not discuss the redox behavior of free porphyr.
Journal ArticleDOI

Kinetics and mechanistic studies of the reactions of metleghemoglobin, ferrylleghemoglobin, and nitrosylleghemoglobin with reactive nitrogen species

TL;DR: It is shown that different forms of Lb react not only with hemoglobin and myoglobin, but also with so-called reactive nitrogen species derived from it, among others peroxynitrite and nitrite, which could contribute to the recycling of these inactive forms to regenerate deoxyLb, the oxygen-binding form of L b.
Journal ArticleDOI

Resonance Raman spectroscopy of protoheme-protein interactions in oxygen-carrying hemoproteins and in peroxidases

TL;DR: Differences observed among resonance Raman spectra show that the proteins of these two classes of hemoprotein impose two distinct heme structures which are likely related to their biological functions, and provides a new understanding of structure-function relationships of protoheme in hemoproteins.
References
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Journal ArticleDOI

Nitrogen fixation by the bacteroid fraction of breis of soybean root nodules

TL;DR: Anaerobically-prepared bacteroids were able to selectively use substrate-generated reducing power for nitrogen fixation instead of for aerobic respiration, although the pO 2 was greater than that necessary to saturate the terminal respiratory pathway.
Journal ArticleDOI

The Kinetics of the Reactions of Leghemoglobin with Oxygen and Carbon Monoxide

TL;DR: It is suggested that leghemoglobin-facilitated oxygen diffusion serves not only to augment the influx of oxygen, but serves as well to make the oxygen pressure within the nodule or cell everywhere nearly the same.
Journal ArticleDOI

Properties of leghaemoglobin in vivo, and its isolation as ferrous oxyleghaemoglobin

TL;DR: Direct spectrophotometry of soybean root nodules under near-physiological conditions establishes that Lb exists in vivo in its ferrous form (Lb2+), which has a myoglobin (Mb)-like spectrum with no haemochrome characteristics.
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