Disparity of native oxyhemoglobin components isolated from Paramecium caudatum and Paramecium primaurelia

Irie, Toshiaki; Usuki, Itaru

doi:10.1016/0305-0491(80)90413-7

Cited by 8 publications

(6 citation statements)

References 15 publications

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“…Optical spectra of ferric Chlamydomonas (8) and Nostoc (9) hemoglobins at neutral pH indicate the presence of a low spin 6-coordinate complex, whereas those of Paramecium (10) and Tetrahymena (7) hemoglobins are consistent with a high spin 6-coordinate conformation reminiscent of the aquo ferric species of myoglobin and hemoglobin.…”

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confidence: 86%

Chlamydomonas Chloroplast Ferrous Hemoglobin

Couture¹,

Das²,

Lee³

et al. 1999

Journal of Biological Chemistry

110

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We report the optical and resonance Raman spectral characterization of ferrous recombinant Chlamydomonas LI637 hemoglobin. We show that it is present in three pH-dependent equilibrium forms including a 4-coordinate species at acid pH, a 5-coordinate high spin species at neutral pH, and a 6-coordinate low spin species at alkaline pH. The proximal ligand to the heme is the imidazole group of a histidine. Kinetics of the reactions with ligands were determined by stopped-flow spectroscopy. At alkaline pH, combination with oxygen, nitric oxide, and carbon monoxide displays a kinetic behavior that is interpreted as being rate-limited by conversion of the 6-coordinate form to a reactive 5-coordinate form. At neutral pH, combination rates of the 5-coordinate form with oxygen and carbon monoxide were much faster (>10 7 M ؊1 s ؊1 ). The dissociation rate constant measured for oxygen is among the slowest known, 0.014 s ؊1 , and is independent of pH. Replacement of the tyrosine 63 (B10) by leucine or of the putative distal glutamine by glycine increases the dissociation rate constant 70-and 30-fold and increases the rate of autoxidation 20-and 90-fold, respectively. These results are consistent with at least two hydrogen bonds stabilizing the bound oxygen molecule, one from tyrosine B10 and the other from the distal glutamine. In addition, the high frequency (232 cm ؊1 ) of the iron-histidine bond suggests a structure that lacks any proximal strain thus contributing to high ligand affinity.

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confidence: 86%

Chlamydomonas Chloroplast Ferrous Hemoglobin

Couture¹,

Das²,

Lee³

et al. 1999

Journal of Biological Chemistry

110

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“…Later, Keilin and Ryley [50] confirmed this by spectroscopic analyses for Paramecium and Tetrahymena. The proteins were purified from P. caudatum [51,52], P. primaurelia [51], P. tetraurelia [53] and T. pyriformis [54]. The molecular mass for the proteins was estimated to be 13-15 kDa, a 10-20% smaller value than usual myoglobin subunit (16)(17)(18).…”

Section: Unicellular Eukaryotesmentioning

confidence: 99%

Evolution of myoglobin

Suzuki

Imai

1998

CMLS, Cell. Mol. Life Sci.

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The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the structures of these proteins suggests that there may be three distinct origins: a 'universal globin', a 'compact globin' and an 'IDO-like globin'.

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confidence: 92%

“…This was later confirmed by Keilin and Ryley with estimations of its content of 1.12 -1.74% [2]. Isolation and characterization of the so-called Paramecium hemoglobin, which is functionally referred to rather as myoglobin [3], have thus been carried out from Paramecium aurelia [4], P. tetraurelia [3], and P. caudatum and P. primaurelia [5].Very recently, we have determined the complete amino acid sequence of a myoglobin isolated from P. caudatum [6]. It consists of 116 amino acid residues with a molecular mass of 12565 Da including the heme moiety, this being much smaller than mammalian myoglobins by 37 residues.…”

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confidence: 92%

Protozoan myoglobin from Paramecium caudatum

Tsubamoto

Matsuoka

et al. 1990

European Journal of Biochemistry

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Native oxymyoglobin (Mb02) was isolated directly from the cells of Paramecium caudatum with complete separation from metmyoglobin (metMb) on a DEAE-cellulose column. It was examined for its spectral and stability properties. When compared with sperm whale MbOz used as a reference, Paramecium MbO, was found to be much more susceptible to autoxidation over a wide range of pH (4-11) in 0.1 M buffer at 25°C. Kinetic analysis has revealed that a proton-catalyzed displacement of 0; from M b 0 2 by an entering water molecule can play a dominant role in the autoxidation reaction of Paramecium Mb02 to metMb, as in the case of sperm whale MbOz involving the distal histidine as its catalytic residue. At pH values higher than 9.5, however, Paramecium MbOz was found to be oxidized to yield a hemichrome. The spontaneous formation of hemichromes is at variance with the other known myoglobins and is therefore discussed in relation to the unusual amino acid sequence of Paramecium myoglobin having a large number of deletion [Iwaasa, H. et al. (1989) J . Mol. Biol. 208,.The occurrence of a hemoglobin-like protein in protozoa was first reported by Sat0 and Tamiya on the basis of spectroscopic observations on cell suspensions of Paramecium caudatum [I]. This was later confirmed by Keilin and Ryley with estimations of its content of 1.12 -1.74% [2]. Isolation and characterization of the so-called Paramecium hemoglobin, which is functionally referred to rather as myoglobin [3], have thus been carried out from Paramecium aurelia [4], P. tetraurelia [3], and P. caudatum and P. primaurelia [5].Very recently, we have determined the complete amino acid sequence of a myoglobin isolated from P. caudatum [6]. It consists of 116 amino acid residues with a molecular mass of 12565 Da including the heme moiety, this being much smaller than mammalian myoglobins by 37 residues. The protein contains two histidine residues at positions 68 and 84, but we failed to find any notable degree of sequence similarity with other known hemoglobins. In relation to these structural studies, the stability properties of the oxygenated form of Paramecium myoglobin should be of most importance and of primary concern, but these are little understood.In this paper, we describe procedures for isolating oxymyoglobin directly from the ciliated cells of P. caudatum and examine for the first time the autoxidation rate of oxymyoglobin (MbO,) to metmyoglobin (metMb) over a wide range of pH values. The resulting pH dependence was subjected to some mechanistic analysis in order to unravel the elementary processes involved in the stability properties of Paramecium MbOz. This kinetic analysis seems to be of great interest when compared with that of sperm whale MbOz as a reference, and should deepen our insight into the myoglobinhemoglobin chemistry and the evolution of these molecules from protozoa to higher animals, since the kinetics of the autoxidation should reflect differences on the distal side of the heme iron [7, 81. Correspondence to K. Shikama, Biological Institute,...

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Disparity of native oxyhemoglobin components isolated from Paramecium caudatum and Paramecium primaurelia

Cited by 8 publications

References 15 publications

Chlamydomonas Chloroplast Ferrous Hemoglobin

Chlamydomonas Chloroplast Ferrous Hemoglobin

Evolution of myoglobin

Protozoan myoglobin from Paramecium caudatum

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