Effect of an Oxygen-Binding Reaction at the Cobalt Porphyrin Site Fixed in a Polymer Membrane on Facilitated Oxygen Transport

1995 ◽  
Vol 68 (3) ◽  
pp. 1036-1041 ◽  
Author(s):  
Takayuki Suzuki ◽  
Yuji Soejima ◽  
Hiroyuki Nishide ◽  
Eishun Tsuchida
Keyword(s):  
Oxygen Transport ◽  
Polymer Membrane ◽  
Oxygen Binding ◽  
Binding Reaction ◽  
Cobalt Porphyrin

Highly Selective Oxygen Transport through a Cobalt Porphyrin Liquid Membrane

1997 ◽  
Vol 101 (29) ◽  
pp. 5725-5729 ◽  
Author(s):  
Xue-Si Chen ◽  
Hiroyuki Nishide ◽  
Kenichi Oyaizu ◽  
Eishun Tsuchida
Keyword(s):  
Oxygen Transport ◽  
Liquid Membrane ◽  
Cobalt Porphyrin

Oxygen transport by rabbit embryonic blood: high cooperativity of hemoglobin-oxygen binding

1995 ◽  
Vol 99 (1) ◽  
pp. 157-164 ◽  
Author(s):  
Robert A.B. Holland ◽  
Susan J. Calvert
Keyword(s):  
Oxygen Transport ◽  
Oxygen Binding

scholarly journals Hemerythrin's oxygen-binding reaction studied by laser photolysis.

1981 ◽  
Vol 78 (4) ◽  
pp. 2307-2309 ◽  
Author(s):  
N. Alberding ◽  
D. Lavalette ◽  
R. H. Austin
Keyword(s):  
Laser Photolysis ◽  
Oxygen Binding ◽  
Binding Reaction

scholarly journals Molecular evolution and expression of oxygen transport genes in livebearing fishes (Poeciliidae) from hydrogen sulfide rich springs

Genome ◽  
2018 ◽  
Vol 61 (4) ◽  
pp. 273-286 ◽  
Author(s):  
Nicholas Barts ◽  
Ryan Greenway ◽  
Courtney N. Passow ◽  
Lenin Arias-Rodriguez ◽  
Joanna L. Kelley ◽  
...  
Keyword(s):  
Gene Expression ◽  
Hydrogen Sulfide ◽  
Molecular Evolution ◽  
Oxygen Transport ◽  
Transport Proteins ◽  
Aquatic Environments ◽  
Oxygen Binding ◽  
The Family ◽  
Signatures Of Selection ◽  
Evolution Of Oxygen

Hydrogen sulfide (H2S) is a natural toxicant in some aquatic environments that has diverse molecular targets. It binds to oxygen transport proteins, rendering them non-functional by reducing oxygen-binding affinity. Hence, organisms permanently inhabiting H2S-rich environments are predicted to exhibit adaptive modifications to compensate for the reduced capacity to transport oxygen. We investigated 10 lineages of fish of the family Poeciliidae that have colonized freshwater springs rich in H2S—along with related lineages from non-sulfidic environments—to test hypotheses about the expression and evolution of oxygen transport genes in a phylogenetic context. We predicted shifts in the expression of and signatures of positive selection on oxygen transport genes upon colonization of H2S-rich habitats. Our analyses indicated significant shifts in gene expression for multiple hemoglobin genes in lineages that have colonized H2S-rich environments, and three hemoglobin genes exhibited relaxed selection in sulfidic compared to non-sulfidic lineages. However, neither changes in gene expression nor signatures of selection were consistent among all lineages in H2S-rich environments. Oxygen transport genes may consequently be predictable targets of selection during adaptation to sulfidic environments, but changes in gene expression and molecular evolution of oxygen transport genes in H2S-rich environments are not necessarily repeatable across replicated lineages.

Effect of Blood Viscosity on Oxygen Transport in Residual Stenosed Artery Following Angioplasty

2008 ◽  
Vol 130 (1) ◽  
Author(s):  
Ohwon Kwon ◽  
Mahesh Krishnamoorthy ◽  
Young I. Cho ◽  
John M. Sankovic ◽  
Rupak K. Banerjee
Keyword(s):  
Flow Rate ◽  
Oxygen Transport ◽  
Blood Viscosity ◽  
Recirculation Zone ◽  
Binding Capacity ◽  
Vasa Vasorum ◽  
Oxygen Binding ◽  
Stenosed Artery ◽  
Hyperemic Flow ◽  
Basal Flow

The effect of blood viscosity on oxygen transport in a stenosed coronary artery during the postangioplasty scenario is studied. In addition to incorporating varying blood viscosity using different hematocrit (Hct) concentrations, oxygen consumption by the avascular wall and its supply from vasa vasorum, nonlinear oxygen binding capacity of the hemoglobin, and basal to hyperemic flow rate changes are included in the calculation of oxygen transport in both the lumen and the avascular wall. The results of this study show that oxygen transport in the postangioplasty residual stenosed artery is affected by non-Newtonian shear-thinning property of the blood viscosity having variable Hct concentration. As Hct increases from 25% to 65%, the diminished recirculation zone for the increased Hct causes the commencement of pO2 decrease to shift radially outward by ∼20% from the center of the artery for the basal flow, but by ∼10% for the hyperemic flow at the end of the diverging section. Oxygen concentration increases from a minimum value at the core of the recirculation zone to over 90mmHg before the lumen-wall interface at the diverging section for the hyperemic flow, which is attributed to increased shear rate and thinner lumen boundary layer for the hyperemic flow, and below 90mmHg for the basal flow. As Hct increases from 25% to 65%, the average of pO2,min beyond the diverging section drops by ∼25% for the basal flow, whereas it increases by ∼15% for the hyperemic flow. Thus, current results with the moderate stenosed artery indicate that reducing Hct might be favorable in terms of increasing O2 flux and pO2,min, in the medial region of the wall for the basal flow, while higher Hct is advantageous for the hyperemic flow beyond the diverging section. The results of this study not only provide significant details of oxygen transport under varying pathophysiologic blood conditions such as unusually high blood viscosity and flow rate, but might also be extended to offer implications for drug therapy related to blood-thinning medication and for blood transfusion and hemorrhage.

Oxygen binding to Arabidopsis thaliana AHb2 nonsymbiotic hemoglobin: evidence for a role in oxygen transport

IUBMB Life ◽  
2011 ◽  
Vol 63 (5) ◽  
pp. 355-362 ◽  
Author(s):  
Francesca Spyrakis ◽  
Stefano Bruno ◽  
Axel Bidon-Chanal ◽  
Francisco Javier Luque ◽  
Stefania Abbruzzetti ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Oxygen Transport ◽  
Oxygen Binding

scholarly journals Cops and robbers: putative evolution of copper oxygen-binding proteins

2000 ◽  
Vol 203 (12) ◽  
pp. 1777-1782 ◽  
Author(s):  
H. Decker ◽  
N. Terwilliger
Keyword(s):  
Immune Response ◽  
Oxygen Transport ◽  
Active Site ◽  
Binding Proteins ◽  
Primary Immune Response ◽  
Evolutionary Relationships ◽  
Oxygen Binding ◽  
Copper Proteins ◽  
Phenoloxidase Activity ◽  
Cops And Robbers

Two closely related copper proteins, phenoloxidase and haemocyanin, are known to be involved in different physiological functions such as the primary immune response and oxygen transport. Although the proteins differ structurally, they have the same active site by which dioxygen is bound. Recent results reveal that haemocyanin also exhibits phenoloxidase activity. A scenario is proposed for the evolutionary relationships among copper oxygen-binding proteins (COPs).

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