Modification of human hemoglobin with methyl acyl phosphates derived from dicarboxylic acids. Systematic relationships between cross-linked structure and oxygen-binding properties

Biochemistry ◽  
1993 ◽  
Vol 32 (1) ◽  
pp. 215-223 ◽  
Author(s):  
Richard T. Jones ◽  
Charlotte G. Head ◽  
Thomas S. Fujita ◽  
Daniel T. B. Shih ◽  
Jolanta Wodzinska ◽  
...  
Keyword(s):  
Dicarboxylic Acids ◽  
Oxygen Binding ◽  
Human Hemoglobin ◽  
Binding Properties ◽  
Systematic Relationships

scholarly journals 3P086 Oxygen binding properties of recombinant human hemoglobin with heme rotational disorder

2005 ◽  
Vol 45 (supplement) ◽  
pp. S225
Author(s):  
Y. Aki-Jin ◽  
S. Nagatomo ◽  
Y. Yamamoto ◽  
M. Nagai ◽  
K. Imai
Keyword(s):  
Oxygen Binding ◽  
Human Hemoglobin ◽  
Binding Properties

Asymmetric Distribution of Cooperativity in the Binding Cascade of Normal Human Hemoglobin. 1. Cooperative and Noncooperative Oxygen Binding in Zn-Substituted Hemoglobin†

Biochemistry ◽  
2005 ◽  
Vol 44 (36) ◽  
pp. 11925-11938 ◽  
Author(s):  
Jo M. Holt ◽  
Alexandra L. Klinger ◽  
Connie S. Yarian ◽  
Varsha Keelara ◽  
Gary K. Ackers
Keyword(s):  
Asymmetric Distribution ◽  
Oxygen Binding ◽  
Human Hemoglobin ◽  
Normal Human

Synthesis and binding properties of calix[4]arene diamide dicarboxylic acids

2000 ◽  
Vol 24 (12) ◽  
pp. 967-972 ◽  
Author(s):  
Françoise Arnaud-Neu ◽  
Silvia Barboso ◽  
Alessandro Casnati ◽  
Alessandra Pinalli ◽  
Marie-Jose´ Schwing-Weill ◽  
...  
Keyword(s):  
Dicarboxylic Acids ◽  
Binding Properties

scholarly journals Haemoglobin polymorphisms affect the oxygen-binding properties in Atlantic cod populations

2008 ◽  
Vol 276 (1658) ◽  
pp. 833-841 ◽  
Author(s):  
Øivind Andersen ◽  
Ola Frang Wetten ◽  
Maria Cristina De Rosa ◽  
Carl Andre ◽  
Cristiana Carelli Alinovi ◽  
...  
Keyword(s):  
Evolutionary Biology ◽  
Quaternary Structure ◽  
Atlantic Cod ◽  
Three Dimensional ◽  
Oxygen Affinity ◽  
Oxygen Binding ◽  
Low Oxygen ◽  
Binding Properties ◽  
Important Species ◽  
The North

A major challenge in evolutionary biology is to identify the genes underlying adaptation. The oxygen-transporting haemoglobins directly link external conditions with metabolic needs and therefore represent a unique system for studying environmental effects on molecular evolution. We have discovered two haemoglobin polymorphisms in Atlantic cod populations inhabiting varying temperature and oxygen regimes in the North Atlantic. Three-dimensional modelling of the tetrameric haemoglobin structure demonstrated that the two amino acid replacements Met55β 1 Val and Lys62β 1 Ala are located at crucial positions of the α 1 β 1 subunit interface and haem pocket, respectively. The replacements are proposed to affect the oxygen-binding properties by modifying the haemoglobin quaternary structure and electrostatic feature. Intriguingly, the same molecular mechanism for facilitating oxygen binding is found in avian species adapted to high altitudes, illustrating convergent evolution in water- and air-breathing vertebrates to reduction in environmental oxygen availability. Cod populations inhabiting the cold Arctic waters and the low-oxygen Baltic Sea seem well adapted to these conditions by possessing the high oxygen affinity Val55–Ala62 haplotype, while the temperature-insensitive Met55–Lys62 haplotype predominates in the southern populations. The distinct distributions of the functionally different haemoglobin variants indicate that the present biogeography of this ecologically and economically important species might be seriously affected by global warming.

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