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Review: Correlations between oxygen affinity and sequence classifications of plant hemoglobins
Author(s) -
Smagghe Benoit J.,
Hoy Julie A.,
Percifield Ryan,
Kundu Suman,
Hargrove Mark S.,
Sarath Gautam,
Hilbert JeanLouis,
Watts Richard A.,
Dennis Elizabeth S.,
Peacock W. James,
Dewilde Sylvia,
Moens Luc,
Blouin George C.,
Olson John S.,
Appleby Cyril A.
Publication year - 2009
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21256
Subject(s) - chemistry , affinities , globin , oxygen , dissociation (chemistry) , stereochemistry , hemoglobin , biochemistry , organic chemistry
Plants express three phylogenetic classes of hemoglobins (Hb) based on sequence analyses. Class 1 and 2 Hbs are full‐length globins with the classical eight helix Mb‐like fold, whereas Class 3 plant Hbs resemble the truncated globins found in bacteria. With the exception of the specialized leghemoglobins, the physiological functions of these plant hemoglobins remain unknown. We have reviewed and, in some cases, measured new oxygen binding properties of a large number of Class 1 and 2 plant nonsymbiotic Hbs and leghemoglobins. We found that sequence classification correlates with distinct extents of hexacoordination with the distal histidine and markedly different overall oxygen affinities and association and dissociation rate constants. These results suggest strong selective pressure for the evolution of distinct physiological functions. The leghemoglobins evolved from the Class 2 globins and show no hexacoordination, very high rates of O 2 binding (∼250 μ M −1 s −1 ), moderately high rates of O 2 dissociation (∼5–15 s −1 ), and high oxygen affinity (K d or P 50 ≈ 50 n M ). These properties both facilitate O 2 diffusion to respiring N 2 fixing bacteria and reduce O 2 tension in the root nodules of legumes. The Class 1 plant Hbs show weak hexacoordination (K HisE7 ≈ 2), moderate rates of O 2 binding (∼25 μ M −1 s −1 ), very small rates of O 2 dissociation (∼0.16 s −1 ), and remarkably high O 2 affinities (P 50 ≈ 2 n M ), suggesting a function involving O 2 and nitric oxide (NO) scavenging. The Class 2 Hbs exhibit strong hexacoordination (K HisE7 ≈ 100), low rates of O 2 binding (∼1 μ M −1 s −1 ), moderately low O 2 dissociation rate constants (∼1 s −1 ), and moderate, Mb‐like O 2 affinities (P 50 ≈ 340 n M ), perhaps suggesting a sensing role for sustained low, micromolar levels of oxygen. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1083–1096, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com