Plant hemoglobins: What we know six decades after their discovery

Garrocho‐Villegas, Verónica; Gopalasubramaniam, Sabarinathan Kuttalingam; Arredondo‐Peter, Raúl

doi:10.1016/j.gene.2007.01.035

Cited by 104 publications

(89 citation statements)

References 70 publications

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“…Understanding the functionality of neuroglobin could provide a paradigm shift in both biology and therapeutics because several highly conserved heme-globins, ubiquitous in plants and animals, exist in equilibrium between dominant six-coordinate heme geometry and a less frequent five-coordinate state. Examples include cytoglobin, cytochrome c, Drosophila melanogaster hemoglobin, and the nonsymbiotic plant hemoglobins (15)(16)(17).…”

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confidence: 99%

Human Neuroglobin Functions as a Redox-regulated Nitrite Reductase

Tiso

Tejero

Basu

et al. 2011

Journal of Biological Chemistry

257

323

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Neuroglobin is a highly conserved hemoprotein of uncertain physiological function that evolved from a common ancestor to hemoglobin and myoglobin. It possesses a six-coordinate heme geometry with proximal and distal histidines directly bound to the heme iron, although coordination of the sixth ligand is reversible. We show that deoxygenated human neuroglobin reacts with nitrite to form nitric oxide (NO). This reaction is regulated by redox-sensitive surface thiols, cysteine 55 and 46, which regulate the fraction of the five-coordinated heme, nitrite binding, and NO formation. Replacement of the distal histidine by leucine or glutamine leads to a stable five-coordinated geometry; these neuroglobin mutants reduce nitrite to NO ϳ2000 times faster than the wild type, whereas mutation of either Cys-55 or Cys-46 to alanine stabilizes the six-coordinate structure and slows the reaction. Using lentivirus expression systems, we show that the nitrite reductase activity of neuroglobin inhibits cellular respiration via NO binding to cytochrome c oxidase and confirm that the six-to-five-coordinate status of neuroglobin regulates intracellular hypoxic NO-signaling pathways. These studies suggest that neuroglobin may function as a physiological oxidative stress sensor and a post-translationally redox-regulated nitrite reductase that generates NO under six-tofive-coordinate heme pocket control. We hypothesize that the sixcoordinate heme globin superfamily may subserve a function as primordial hypoxic and redox-regulated NO-signaling proteins.

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mentioning

confidence: 99%

Human Neuroglobin Functions as a Redox-regulated Nitrite Reductase

Tiso

Tejero

Basu

et al. 2011

Journal of Biological Chemistry

257

323

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“…The monomeric units of animal and plant hemoglobins fold into a highly conserved globin-type structure. Both symbiotic and non-symbiotic hemoglobins have been found in dicotyledons (Trevaskis et al, 1997), while only non-symbiotic hemoglobins have been detected in monocotyledons (Figure 1) Garrocho-Villegas et al, 2007). It has been reported that genes of symbiotic and nonsymbiotic hemoglobins have three introns and four exons (Arredondo-Peter et al, 1998).…”

Section: Evolution Of Plant Hemoglobinsmentioning

confidence: 90%

“…At the beginning of the 21 st century, another type of hemoglobin was found in Arabidopsis with structural similarities to bacteria, protozoan, and algae hemoglobin Wittenberg et al, 2002); it is therefore known as truncated hemoglobin. To date more than 50 plant hemoglobins have been found in over 20 species (Garrocho-Villegas et al, 2007;BustosSanmamed et al, 2011;Bhattacharya et al, 2013).…”

Section: Historical Overview Of Plant Hemoglobinsmentioning

confidence: 99%

“…NsHbs are widely distributed in the plant kingdom while symbiotic hemoglobins are restricted to the nodules of N-fixing plants, which suggests that the latter arose from a duplication of a hemoglobin gene in which one of the copies was sequestered to perform a specific function in the nodules (Appleby, 1992). Since then the two types Source: Garrocho-Villegas et al (2007) and Thompson et al (1997). of plant hemoglobins have evolved independently with different functions.…”

Section: Evolution Of Plant Hemoglobinsmentioning

confidence: 99%

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Non-symbiotic hemoglobin and its relation with hypoxic stress

Riquelme¹,

Hinrichsen

2015

Chilean J. Agric. Res.

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Today we know that several types of hemoglobins exist in plants. The symbiotic hemoglobins were discovered in 1939 and are only found in nodules of plants capable of symbiotically fixing atmospheric N. Another class, called non-symbiotic hemoglobin, was discovered 32 yr ago and is now thought to exist throughout the plant kingdom, being expressed in different organs and tissues. Recently the existence of another type of hemoglobin, called truncated hemoglobin, was demonstrated in plants. Although the presence of hemoglobins is widespread in the plant kingdom, their role has not yet been fully elucidated. This review discusses recent findings regarding the role of plant hemoglobins, with special emphasis on their relationship to plants adaptation to hypoxia. It also discusses the role of nitric oxide in plant cells under hypoxic conditions, since one of the functions of hemoglobin appears to be modulating nitric oxide levels in the cells.

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“…A major event during the evolution of land plant nsHbs was the duplication of an ancestral nshb into nshb-1 and nshb-2 prior to the monocot-dicot divergence 18, 148 . Sequence analysis revealed that nshb-1 and nshb-2 genes exist in dicots and that apparently only nshb-1 genes exist in monocots 9, 94, 149 . Earlier Garrocho-Villegas and co-workers 75 reported the existence of a nsHb (Hb5) divergent from rice (Hb1 to 4) nsHbs-1 and suggested that nsHbs divergent from nsHbs-1 evolved within monocots.…”

Section: Evolution Of Rice Hemoglobinsmentioning

confidence: 99%

Rice (Oryza) hemoglobins

2014

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Hemoglobins (Hbs) corresponding to non-symbiotic (nsHb) and truncated (tHb) Hbs have been identified in rice ( Oryza). This review discusses the major findings from the current studies on rice Hbs. At the molecular level, a family of the nshb genes, consisting of hb1, hb2, hb3, hb4 and hb5, and a single copy of the thb gene exist in Oryza sativa var. indica and O. sativa var. japonica, Hb transcripts coexist in rice organs and Hb polypeptides exist in rice embryonic and vegetative organs and in the cytoplasm of differentiating cells. At the structural level, the crystal structure of rice Hb1 has been elucidated, and the structures of the other rice Hbs have been modeled. Kinetic analysis indicated that rice Hb1 and 2, and possibly rice Hb3 and 4, exhibit an extremely high affinity for O 2, whereas rice Hb5 and tHb possibly exhibit a low to moderate affinity for O 2. Based on the accumulated information on the properties of rice Hbs and data from the analysis of other plant and non-plant Hbs, it is likely that Hbs play a variety of roles in rice organs, including O 2-transport, O 2-sensing, NO-scavenging and redox-signaling. From an evolutionary perspective, an outline for the evolution of rice Hbs is available. Rice nshb and thb genes vertically evolved through different lineages, rice nsHbs evolved into clade I and clade II lineages and rice nshbs and thbs evolved under the effect of neutral selection. This review also reveals lacunae in our ability to completely understand rice Hbs. Primary lacunae are the absence of experimental information about the precise functions of rice Hbs, the properties of modeled rice Hbs and the cis-elements and trans-acting factors that regulate the expression of rice hb genes, and the partial understanding of the evolution of rice Hbs.

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Plant hemoglobins: What we know six decades after their discovery

Cited by 104 publications

References 70 publications

Human Neuroglobin Functions as a Redox-regulated Nitrite Reductase

Human Neuroglobin Functions as a Redox-regulated Nitrite Reductase

Non-symbiotic hemoglobin and its relation with hypoxic stress

Rice (Oryza) hemoglobins

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