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 …

New developments have forced a re-evaluation of our understanding of the structure and
function of hemoglobins. Leghemoglobins regulate oxygen affinity through a mechanism …

Plant hemoglobins constitute a diverse group of hemeproteins and evolutionarily belong to
three different classes. Class 1 hemoglobins possess an extremely high affinity to oxygen …

Nonsymbiotic hemoglobins (nsHbs) are widespread in plants including bryophytes.
Bryophytes (such as mosses) are among the oldest land plants, thus an analysis of a …

The evolution of oxygen transport hemoglobins occurred on at least two independent
occasions. The earliest event led to myoglobin and red blood cell hemoglobin in animals. In …

Plants, like humans, contain hemoglobin. Three distinct types of hemoglobin exist in plants:
symbiotic, non-symbiotic, and truncated hemoglobins. Crystal structures and other structural …

All plants contain an unusual class of hemoglobins that display bis-histidyl coordination yet
are able to bind exogenous ligands such as oxygen. Structurally homologous …

Background: Nonsymbiotic hemoglobins (nsHbs) form a new class of plant proteins that is
distinct genetically and structurally from leghemoglobins. They are found ubiquitously in …

Nonsymbiotic class 1 plant hemoglobins are induced under hypoxia. Structurally they are
protein dimers consisting of two identical subunits, each containing heme iron in a weak …

Plant nonsymbiotic hemoglobins are hexacoordinate heme proteins found in all plants.
Although expression is linked with hypoxic environmental conditions (Taylor, ER, Nie, XZ …