Evolution of cooperativity in hemoglobins: What can invertebrate hemoglobins tell us?

Kitto, G. Barrie; Thomas, Pei W.; Hackert, Marvin L.

doi:10.1002/(sici)1097-010x(199809/10)282:1/2<120::aid-jez13>3.0.co;2-y

Cited by 10 publications

(3 citation statements)

References 22 publications

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“…On the proximal side, the azimuthal orientation of the HisF8 imidazole ring is determined, in monomeric hemichrome HbC, by a strong hydrogen bond to residue TyrG5; this interaction is absent in the ferric cyanide derivative of dimeric HbD. Interestingly, the aggregation state of C. arenicola Hbs is unusually ligand-linked, possibly underlying a signal transduction mechanism (48)(49)(50)(51).…”

Section: The Hexa-coordinate Heme In the Hb Superfamilysupporting

confidence: 53%

“…While whole coelomic cells and cell lysates show moderate cooperativity (n 50 = 1.4) in O 2 binding, and P 50 of approximately 9 torr, the single globin types (i.e., A, B, C, and D chains) exhibit greater O 2 affinity (P 50 = 2 -3 torr) but still exhibit measurable cooperativity. Interestingly, a marked increase in cooperativity has been observed when the D globin was added to any of the other three chains (51,66).…”

Section: Ligand Binding To Hexa-coordinate Globinsmentioning

confidence: 99%

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Structure‐Function Relationships in the Growing Hexa‐Coordinate Hemoglobin Sub‐Family

Sanctis¹,

Pesce²,

Nardini

et al. 2004

IUBMB Life

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SummaryHemoglobin and related heme proteins, generally referred to as 'globins', reversibly bind gaseous diatomic ligands (O 2 , NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexacoordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa-to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties. IUBMB Life, 56: 643-651, 2004

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Section: The Hexa-coordinate Heme In the Hb Superfamilysupporting

confidence: 53%

Section: Ligand Binding To Hexa-coordinate Globinsmentioning

confidence: 99%

Structure‐Function Relationships in the Growing Hexa‐Coordinate Hemoglobin Sub‐Family

Sanctis¹,

Pesce²,

Nardini

et al. 2004

IUBMB Life

View full text Add to dashboard Cite

show abstract

“…The single chains exhibit slight but measurable cooperativity and high affinity (P 50 ϭ 2-3 Torr). Affinity falls and cooperativity increases markedly when the D chain is added to any of the other three chains (300).…”

Section: Echinodermsmentioning

confidence: 99%

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Weber

Vinogradov

2001

Physiological Reviews

453

404

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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 O(2) 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 O(2) in nematodes, binding and transport of sulfide in endosymbiont-harboring species and protection against sulfide, scavenging of O(2 )in symbiotic leguminous plants, O(2 )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 O(2 )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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Exploring and exploiting allostery: Models, evolution, and drug targeting

Peracchi

Mozzarelli

2011

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Evolution of cooperativity in hemoglobins: What can invertebrate hemoglobins tell us?

Cited by 10 publications

References 22 publications

Structure‐Function Relationships in the Growing Hexa‐Coordinate Hemoglobin Sub‐Family

Structure‐Function Relationships in the Growing Hexa‐Coordinate Hemoglobin Sub‐Family

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Exploring and exploiting allostery: Models, evolution, and drug targeting

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