A globin in every cell?

Riggs, Austen; Gorr, Thomas A.

doi:10.1073/pnas.0600290103

Cited by 18 publications

(13 citation statements)

References 24 publications

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“…Although there are several studies on the expression and regulation of Ngb (Burmester and Hankeln, 2004;Roesner et al, 2008), its role in the adaptation of the goldfish to hypoxia is still poorly understood. Some studies (Bentmann et al, 2005) suggest that Ngb may facilitate O 2 delivery just like Mb whereas others (Fraser et al, 2006;Riggs and Gorr, 2006) believe that it may play a role in the detoxification of reactive nitrogen (RNS) and reactive oxygen species (ROS) and hypoxia-related signaling (Fago et al, 2006). Our results lend support to the latter proposition and we believe that Ngb and Mb may complement/supplement the antioxidants in the detoxification of RNS and ROS.…”

Section: Discussionsupporting

confidence: 71%

Organ-dependent response in antioxidants, myoglobin and neuroglobin in goldfish (Carassius auratus) exposed to MC-RR under varying oxygen level

et al. 2014

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Section: Discussionsupporting

confidence: 71%

Organ-dependent response in antioxidants, myoglobin and neuroglobin in goldfish (Carassius auratus) exposed to MC-RR under varying oxygen level

et al. 2014

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“…Globins came into being during the planet's long early period of anoxia/hypoxia, and recent studies show that globins are either expressed or inducible in almost all cells (98). Studies have shown that one evolutionary pathway of Hb is that of a multipurpose domain attached to a variety of unrelated proteins, thus forming molecules with different functions (126).…”

Section: General Principlesmentioning

confidence: 99%

Molecular Controls of the Oxygenation and Redox Reactions of Hemoglobin

Bonaventura

Henkens

Alayash

et al. 2013

Antioxidants & Redox Signaling

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Significance: The broad classes of O 2 -binding proteins known as hemoglobins (Hbs) carry out oxygenation and redox functions that allow organisms with significantly different physiological demands to exist in a wide range of environments. This is aided by allosteric controls that modulate the protein's redox reactions as well as its O 2 -binding functions. Recent Advances: The controls of Hb's redox reactions can differ appreciably from the molecular controls for Hb oxygenation and come into play in elegant mechanisms for dealing with nitrosative stress, in the malarial resistance conferred by sickle cell Hb, and in the as-yet unsuccessful designs for safe and effective blood substitutes. Critical Issues: An important basic principle in consideration of Hb's redox reactions is the distinction between kinetic and thermodynamic reaction control. Clarification of these modes of control is critical to gaining an increased understanding of Hb-mediated oxidative processes and oxidative toxicity in vivo. Future Directions: This review addresses emerging concepts and some unresolved questions regarding the interplay between the oxygenation and oxidation reactions of structurally diverse Hbs, both within red blood cells and under acellular conditions. Developing methods that control Hbmediated oxidative toxicity will be critical to the future development of Hb-based blood substitutes. Antioxid. Redox Signal. 18, 2298-2313. General PrinciplesEmergence of proteins capable of transporting O 2 I n this review, we examine the adaptive changes in the molecular controls of hemoglobin (Hb) oxygenation and oxidation that have evolved to meet the highly varied physiological and environmental demands of respiring organisms. Globins came into being during the planet's long early period of anoxia/hypoxia, and recent studies show that globins are either expressed or inducible in almost all cells (98). Studies have shown that one evolutionary pathway of Hb is that of a multipurpose domain attached to a variety of unrelated proteins, thus forming molecules with different functions (126). This pathway has allowed structurally distinct Hbs to evolve: (i) to protect against the high levels of nitrosative stress of the earth's early environment; (ii) to protect against O 2 -linked oxidation; (iii) to act as O 2 sensors that help regulate the expression of proteins during periods of hypoxia or anoxia; and (iv) to enable aerobic respiration by facilitating diffusion and/or acting as O 2 carriers (44,56,57,70,71,73,107). A common theme in the fascinating story of Hb evolution is the emergence of distinct mechanisms for controlling Hb's oxygenation and redox functions.Since increased amounts of O 2 were released in our planet's early history, O 2 toxicity brought about species extinction on a global scale. On the other hand, this ''oxygen pollution'' made possible a new biological process, that of aerobic respiration. A tremendous gain in the energy obtainable from oxidation of energy-rich metabolites was achieved when organisms evolve...

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“…Multiple globins are also normally expressed in non-erythroid vertebrate cells and tissues [4, 5], and globin expression is deranged in cancer cells [6–9]. When asking the question “what are all these oxygen-binding heme proteins doing?” [10], investigators are now obliged to thoroughly consider enzyme functions, and in particular a NOD function

\begin{matrix} NO + O_{normal2} + e^{-} \to {NO}_{normal3}^{-} \end{matrix}

…”

Section: Background and Introductionmentioning

confidence: 99%

Hemoglobin: A Nitric-Oxide Dioxygenase

Gardner

2012

Scientifica

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Members of the hemoglobin superfamily efficiently catalyze nitric-oxide dioxygenation, and when paired with native electron donors, function as NO dioxygenases (NODs). Indeed, the NOD function has emerged as a more common and ancient function than the well-known role in O2 transport-storage. Novel hemoglobins possessing a NOD function continue to be discovered in diverse life forms. Unique hemoglobin structures evolved, in part, for catalysis with different electron donors. The mechanism of NOD catalysis by representative single domain hemoglobins and multidomain flavohemoglobin occurs through a multistep mechanism involving O2 migration to the heme pocket, O2 binding-reduction, NO migration, radical-radical coupling, O-atom rearrangement, nitrate release, and heme iron re-reduction. Unraveling the physiological functions of multiple NODs with varying expression in organisms and the complexity of NO as both a poison and signaling molecule remain grand challenges for the NO field. NOD knockout organisms and cells expressing recombinant NODs are helping to advance our understanding of NO actions in microbial infection, plant senescence, cancer, mitochondrial function, iron metabolism, and tissue O2 homeostasis. NOD inhibitors are being pursued for therapeutic applications as antibiotics and antitumor agents. Transgenic NOD-expressing plants, fish, algae, and microbes are being developed for agriculture, aquaculture, and industry.

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A globin in every cell?

Cited by 18 publications

References 24 publications

Organ-dependent response in antioxidants, myoglobin and neuroglobin in goldfish (Carassius auratus) exposed to MC-RR under varying oxygen level

Organ-dependent response in antioxidants, myoglobin and neuroglobin in goldfish (Carassius auratus) exposed to MC-RR under varying oxygen level

Molecular Controls of the Oxygenation and Redox Reactions of Hemoglobin

Hemoglobin: A Nitric-Oxide Dioxygenase

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