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Physiological Reviews, Vol. 81, No. 2, April 2001, pp. 569-628
Copyright ©2001 by the American Physiological Society
Danish Centre for Respiratory Adaptation, Department of Zoophysiology, Institute of Biology, University of Aarhus, Aarhus, Denmark; and Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan
Weber, Roy E. and
Serge N. Vinogradov.
Nonvertebrate Hemoglobins: Functions and Molecular
Adaptations. Physiol. Rev. 81: 569-628, 2001.
Hemoglobin (Hb) occurs in all the
kingdoms of living organisms. Its distribution is episodic among the
nonvertebrate groups in contrast to vertebrates. Nonvertebrate Hbs
range from single-chain globins found in bacteria, algae, protozoa,
and plants to large, multisubunit, multidomain Hbs found in nematodes,
molluscs and crustaceans, and the giant annelid and vestimentiferan Hbs
comprised of globin and nonglobin subunits. Chimeric hemoglobins have
been found recently in bacteria and fungi. Hb occurs intracellularly in
specific tissues and in circulating red blood cells (RBCs) and freely
dissolved in various body fluids. In addition to transporting and
storing O2 and facilitating its diffusion, several novel Hb functions have emerged, including control of nitric oxide (NO) levels
in microorganisms, use of NO to control the level of O2 in
nematodes, binding and transport of sulfide in
endosymbiont-harboring species and protection against sulfide,
scavenging of O2 in symbiotic leguminous plants, O2
sensing in bacteria and archaebacteria, and dehaloperoxidase
activity useful in detoxification of chlorinated materials. This review
focuses on the extensive variation in the functional properties of
nonvertebrate Hbs, their O2 binding affinities, their
homotropic interactions (cooperativity), and the sensitivities of these
parameters to temperature and heterotropic effectors such as protons
and cations. Whenever possible, it attempts to relate the ligand
binding properties to the known molecular structures. The divergent and
convergent evolutionary trends evident in the structures and functions
of nonvertebrate Hbs appear to be adaptive in extending the inhabitable
environment available to Hb-containing organisms.
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