The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps

Crystal structures of hemoglobin (Hb) from two flightless birds, ostrich (Struthio camelus) and turkey (Meleagris gallopova), were determined. The ostrich Hb structure was solved to a resolution of 2.22 Å, whereas two forms of turkey Hb were solved to resolutions of 1.66 Å (turkey monoclinic structure; TMS) and 1.39 Å (turkey orthorhombic structure; TOS). Comparison of the amino-acid sequences of ostrich and turkey Hb with those from other avian species revealed no difference in the number of charged residues, but variations were observed in the numbers of hydrophobic and polar residues. Amino-acid-composition-based computation of various physical parameters, in particular their lower inverse transition temperatures and higher average hydrophobicities, indicated that the structures of ostrich and turkey Hb are likely to be highly ordered when compared with other avian Hbs. From the crystal structure analysis, the liganded state of ostrich Hb was confirmed by the presence of an oxygen molecule between the Fe atom and the proximal histidine residue in all four heme regions. In turkey Hb (both TMS and TOS), a water molecule was bound instead of an oxygen molecule in all four heme regions, thus confirming that they assumed the aqua-met form. Analysis of tertiary- and quaternary-structural features led to the conclusion that ostrich oxy Hb and turkey aqua-met Hb adopt the R-/RH-state conformation.

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Oxygen Binding of Monotreme Haemoglobins I. Oxygen Binding Parameters of the Haemoglobins of Platypus, Ornithorhynchus anatinus, and Echidna, Tachyglossus aculeatus

Australian Journal of Biological Sciences ◽

10.1071/bi9780327 ◽

1978 ◽

Vol 31 (4) ◽

pp. 327 ◽

Cited By ~ 1

Author(s):

RW Hosken

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Saturation Pressure ◽

Oxygen Affinity ◽

Steric Effects ◽

Oxygen Binding ◽

Binding Parameters ◽

Ph Values ◽

Ornithorhynchus Anatinus ◽

Lower Oxygen

Oxygen binding parameters have been determined for echidna and platypus haemolysates. At pH 7� 1 and 25�C platypus haemoglobin with an oxygen half-saturation pressure (Pso) of 2�4 kPa has a lower oxygen affinity than echidna haemoglobin with a Pso of 1�6 kPa. The AHo of oxygenation of platypus haemoglobin is -38�9kJ/mol which is more exothermic than the -29�7kJ/mol of echidna haemoglobin. Platypus haemoglobin has a steeper alkaline Bohr curve than echidna haemoglobin, while both haemoglobins show high levels of cooperativity at various temperatures and pH values. It appears that diphosphoglyceric acid modulates the affinity of echidna and platypus haemoglobins to different extents. This information is interpreted in terms of the steric effects of ligand binding originating in the amino acid sequence differences of these two species.

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Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli

Biochemical Journal ◽

10.1042/bj2880649 ◽

1992 ◽

Vol 288 (2) ◽

pp. 649-655 ◽

Cited By ~ 55

Author(s):

N Ioannidis ◽

C E Cooper ◽

R K Poole

Keyword(s):

Escherichia Coli ◽

Amino Acid ◽

Amino Acid Sequence ◽

Molecular Mass ◽

Spectroscopic Studies ◽

Oxygen Binding ◽

Histidine Residue ◽

Nitrosyl Complex ◽

Sds Page ◽

Prosthetic Groups

The Escherichia coli haemoglobin-like flavohaemoprotein (Hmp) has been purified to near homogeneity using two chromatographic steps. The prosthetic groups are identified as FAD and protohaem IX. SDS/PAGE has indicated a molecular mass of 44 kDa for the monomeric protein consistent with the amino-acid sequence deduced from the hmp+ gene. The protein, as isolated, is in the Fe(III) state, exhibiting absorbance maxima at 403.5, 540 (shoulder) and 627 nm. The ferrous and carbonmonoxyferrous states resemble those of haemoglobin, showing maxima at 431.5 and 558 nm, and 421, 542 and 566 nm respectively. Upon aerobic addition of NAD(P)H, the ferric state is reduced to the oxygenated Fe(II) state, characterized by maxima at 413, 544 and 580 nm. This oxy form is not stable and slowly decays to the ferric state. Addition of dithionite and nitrite to the ferric protein results in the formation of a nitrosyl complex, whose e.p.r. characteristics indicate that the b-type haem is attached to the protein through a nitrogenous ligand, probably originating from a histidine residue.

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P3-039: Aβ binding properties of a synthetic peptide corresponding to an amino acid sequence in human pericentriolar material 1 (PCM-1) protein

Alzheimer s & Dementia ◽

10.1016/j.jalz.2012.05.1257 ◽

2012 ◽

Vol 8 (4S_Part_13) ◽

pp. P469-P469

Author(s):

Balu Chakravarthy ◽

Trevor Atkinson ◽

Leslie Brown ◽

Michel Menard ◽

Shingo Ito ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Synthetic Peptide ◽

Binding Properties ◽

Pericentriolar Material

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The Amino Acid Sequence and Copper(II)-binding Properties of Peptide (1–24) of Bovine Serum Albumin

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)99380-4 ◽

1967 ◽

Vol 242 (23) ◽

pp. 5451-5459 ◽

Cited By ~ 9

Author(s):

William T. Shearer ◽

Ralph A. Bradshaw ◽

Frank R.N. Gurd ◽

Peters Theodore

Keyword(s):

Amino Acid ◽

Bovine Serum Albumin ◽

Amino Acid Sequence ◽

Serum Albumin ◽

Bovine Serum ◽

Binding Properties

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Analysis of Interhexameric Contact Regions in Two Dodecameric Hemocyanins at Subdohain Resolution by Combination of Data from Electron Microscopy, X-Ray Diffraction and Amino-Acid Sequence Studies

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100180082 ◽

1990 ◽

Vol 48 (1) ◽

pp. 266-267

Author(s):

Felix de Haas ◽

Jan F. L. van Breemen ◽

Martha M. C. Bijlholt ◽

Ernst F. J. van Bruggen

Keyword(s):

Amino Acid ◽

Molecular Assembly ◽

Oxygen Binding ◽

X Ray Diffraction ◽

Biological Macromolecule ◽

Binding Properties ◽

X Ray ◽

Simulation Procedure ◽

Cancer Pagurus ◽

The Difference

Hemocyanin is a biological macromolecule which occurs freely dissolved in the hemolymph of certain invertebrates. The function of this copper containing protein is the transport of oxygen through the organism. In fulfilling this task hemocyanin has developed a similar mechanism as hemoglobin in binding oxygen reversibly and cooperatively. The hemocyanin of arthropods consists of one or more hexamers of subunits with a molecular weight of approx. 75 000. Depending on the species 3-15 types of monomeric subunits occur, which differ in amino-acid composition and in their oxygen binding properties. Each type of subunit fulfills a specific role in the architecture of that hemocyanin. In nature arthropodan hemocyanin is found as a one-hexameric, two-hexameric (dodecameric), four-hexameric or eight-hexameric molecular assembly depending on the species. In this work we focus on the difference in organization of the hexamers in the dodecamer of two different species i.e. the tarantula Eurypelma californicum (a chelicerate) and the crab Cancer pagurus (a crustacean). Eurypelma hemocyanin is made from 7 different subunits called a - g, whereas Cancer hemocyanin consists of 3 subunit types termed α, β, and γ .By image analysis of electron micrographs of the two-hexameric half hemocyanin molecules from Eurypelma and the two-hexameric whole hemocyanin molecules from Cancer, computer averaged projections of these dodecamers were obtained as shown in fig. 1. They differ clearly in their interhexameric contacts. To analyse this difference in more detail these projections were used as a reference in a simulation procedure.

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Amino acid sequence and some ligand binding properties of fatty acid-binding protein from bovine brain

Cellular Fatty Acid-binding Proteins ◽

10.1007/978-1-4615-3936-0_5 ◽

1990 ◽

pp. 35-39

Author(s):

F. Schoentgen ◽

L. M. Bonanno ◽

G. Pignède ◽

P. Jollès

Keyword(s):

Fatty Acid ◽

Amino Acid ◽

Amino Acid Sequence ◽

Ligand Binding ◽

Fatty Acid Binding Protein ◽

Binding Protein ◽

Bovine Brain ◽

Binding Properties ◽

Fatty Acid Binding ◽

Acid Binding Protein

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An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences

Biochemical Journal ◽

10.1042/bj2870957 ◽

1992 ◽

Vol 287 (3) ◽

pp. 957-963 ◽

Cited By ~ 125

Author(s):

S E Pemble ◽

J B Taylor

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Amino Acid Sequence Identity ◽

Glutathione Transferase ◽

Glutathione Transferases ◽

Purple Bacterium ◽

Binding Properties ◽

Cdna Sequences ◽

Sequence Identity ◽

High Conservation

We report the cDNA sequence for rat glutathione transferase (GST) subunit 5, which is one of at least three class Theta subunits in this species. This sequence, when compared with that of subunit 12 recently published by Ogura, Nishiyama, Okada, Kajita, Narihata, Watabe, Hiratsuka & Watabe [(1991) Biochem. Biophys. Res. Commun. 181, 1294-1300] proves that Theta is a separate multigene class of GST with little amino acid sequence identity with Mu-, Alpha- or Pi-class enzymes. The amino acid sequence identity of class-Theta subunits is highly conserved in rat, the fruitfly Drosophila, maize (Zea mays) and Methylobacterium, which suggests that this family is representative of the ancient progenitor GST gene and originates from the endosymbioses of a purple bacterium leading to the mitochondrion. The high conservation of class Theta brings into prominence that Alpha-, Mu- and Pi-class enzymes, which are not present in plants, derive from a Theta-class gene duplication before the divergence of fungi and animals and, given the binding properties of the Alpha-, Mu- and Pi-classes, suggests a role for these in the evolution of fungi and animals.

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