Cold-adapted enzymes

CJ Marshall - Trends in biotechnology, 1997 - cell.com
It is an article of faith among biochemists and molecular biologists that precious enzymes
must be stored on ice. The usual reason given is that, at temperatures around freezing …

Root effect hemoglobins

T Brittain - Journal of inorganic biochemistry, 2005 - Elsevier
The Root effect describes an extreme pH sensitivity expressed in the hemoglobins of certain
fish, in which it plays a unique physiological role. This review describes our general …

Mathematical elegance with biochemical realism: the covarion model of molecular evolution

D Penny, BJ McComish, MA Charleston… - Journal of Molecular …, 2001 - Springer
There is an apparent paradox in our understanding of molecular evolution. Current
biochemically based models predict that evolutionary trees should not be recoverable for …

Hemoglobin structure and function

FB Jensen, A Fago, RE Weber - Fish physiology, 1998 - Elsevier
Transport of oxygen from the environment to cells and transport of metabolically produced
carbon dioxide and H+ in the opposite direction are essential for vertebrate life. Hemoglobin …

Cold-driven hemoglobin evolution in Antarctic notothenioid fishes prior to hemoglobin gene loss in white-blooded icefishes

T Desvignes, I Bista, K Herrera, A Landes… - Molecular Biology …, 2023 - academic.oup.com
Expression of multiple hemoglobin isoforms with differing physiochemical properties likely
helps species adapt to different environmental and physiological conditions. Antarctic …

Non-functional conserved residues in globins and their possible role as a folding nucleus

OB Ptitsyn, KLH Ting - Journal of molecular biology, 1999 - Elsevier
Structure-based sequence alignment of 728 sequences of different globin subfamilies
shows that in each subfamily there are two clusters of consensually conserved residues. The …

The crystal structure of a tetrameric hemoglobin in a partial hemichrome state

A Riccio, L Vitagliano, G di Prisco… - Proceedings of the …, 2002 - National Acad Sciences
Tetrameric hemoglobins are the most widely used systems in studying protein cooperativity.
Allosteric effects in hemoglobins arise from the switch between a relaxed (R) state and a …

Structure of deoxyhaemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and …

N Ito, NH Komiyama, G Fermi - Journal of molecular biology, 1995 - Elsevier
We have determined the structure of deoxyhaemoglobin from the antarctic fishPagothenia
bernacchiiat pH 6.2 to a resolution of 2.2 Å with X-ray data from a twinned crystal …

The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)

J Zhang, Z Hua, JRH Tame, G Lu, R Zhang… - Journal of molecular …, 1996 - Elsevier
We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form
to a resolution of 2.0 Å. TheR-factor of the model is 19.8%. The structure is similar to human …

Structural basis for the Root effect in haemoglobin

SE Mylvaganam, C Bonaventura… - Nature Structural …, 1996 - nature.com
The remarkable ability of Root effect haemoglobins to pump oxygen against high O2
gradients results from extreme, acid-induced reductions in O2 affinity and cooperativity. The …