[7] Preparation and characterization of insect hemoglobins from Chironomus thummi thummi

Ruf, Hans Heinrich; Altemüller, Andreas G.; Gersonde, Klaus

doi:10.1016/0076-6879(94)31009-2

Cited by 10 publications

(7 citation statements)

References 46 publications

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“…Native C. thummi thummi Hbs possessing protohemin IX (Fig. 1) were prepared as described previously [7,14,261. The cyanide complexes were prepared by adding =lO-fold excess of KCN to Hb solutions.…”

Section: Methodsmentioning

confidence: 99%

Solution ¹H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Zhang¹,

Mar²,

Gersonde³

1996

European Journal of Biochemistry

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Solution 1H‐NMR studies of the heme cavity were performed for the cyanomet complexes of monomeric hemoglobins III and IV from the insect Chironomus thummi thummi, each of which exhibit marked Bohr effects. The low pH 5, paramagnetic (S= 1/2) derivatives were selected for study because the large dipolar shifts provide improved resolution over diamagnetic forms and allow distinction between the two isomeric heme orientations [Peyton, D. H., La Mar, G. N. & Gersonde, K. (1988) Biochim. Biophys. Acta 954, 82–94]. The crystal structure for the low‐pH form of the hemoglobin III derivative, moreover, has been reported and showed that the functionally implicated distal His58 side chain adopts alternative orientations, either in or out of the pocket [Steigemann, W. & Weber, E. (1979) J. Mol. Biol. 127, 309–338]. All heme pocket residues for the low‐pH forms of the two hemoglobins were located, at least in part, and positioned in the heme cavity on the basis of nuclear Overhauser effects to the heme and each other, dipolar shifts, and paramagnetic‐induced relaxation. The resulting structure yielded the orientation of the major axis of the paramagnetic susceptibility tensor. The heme pocket structure of the cyanomet hemoglobins III and IV were found to be indistinguishable, with both exhibiting a distal His58 oriented solely into the heme cavity and in contact with the ligand, and with two residues, Phe100 and Phe38, exhibiting small but significant displacements in solution relative to hemoglobin III in the crystal.

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Section: Methodsmentioning

confidence: 99%

Solution ¹H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Zhang¹,

Mar²,

Gersonde³

1996

European Journal of Biochemistry

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“…Some important work has been conducted on the physiology and molecular biology of these insects. For example, the diversity of hemolymphatic hemoglobins, which constitutes a characteristic feature of chironomids, has been investigated in detail (Ruf et al, 1994;Hankeln et al, 1998), mainly within the genus Chironomus (Fig. 1A).…”

Section: Introductionmentioning

confidence: 99%

Chironomid Midges (Diptera, Chironomidae) Show Extremely Small Genome Sizes

et al. 2015

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“…It is a vital nutrient for most, if not all, insects for their embryonic development [20], although they do not use it as a transport vehicle or storage vessel for oxygen. Heme also serves as the prosthetic moiety of hemoproteins, such as hemoglobin [21,22], catalase [23] and nitric oxide synthase [24], which are essential for biological function. However, heme is potentially toxic to insects, particularly blood‐sucking insects such as mosquitoes, because it catalyzes oxidative reactions that can damage membranes and destroy nucleic acids.…”

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confidence: 99%

Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied

Zhang¹,

Sato

Sasahara³

et al. 2004

European Journal of Biochemistry

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We cloned a cDNA for a Drosophila melanogaster homologue of mammalian heme oxygenase (HO) and constructed a bacterial expression system of a truncated, soluble form of D. melanogaster HO (DmDHO). The purified DmDHO degraded hemin to biliverdin, CO and iron in the presence of reducing systems such as NADPH/cytochrome P450 reductase and sodium ascorbate, although the reaction rate was slower than that of mammalian HOs. Some properties of DmHO, however, are quite different from other known HOs. Thus DmDHO bound hemin stoichiometrically to form a hemin-enzyme complex like other HOs, but this complex did not show an absorption spectrum of hexacoordinated heme protein. The absorption spectrum of the ferric complex was not influenced by changing the pH of the solution. Interestingly, an EPR study revealed that the iron of heme was not involved in binding heme to the enzyme. Hydrogen peroxide failed to convert it into verdoheme. A spectrum of the ferrous-CO form of verdoheme was not detected during the reaction from hemin under oxygen and CO. Degradation of hemin catalyzed by DmDHO yielded three isomers of biliverdin, of which biliverdin IXa and two other isomers (IXb and IXd) accounted for 75% and 25%, respectively. Taken together, we conclude that, although DmHO acts as a real HO in D. melanogaster, its active-site structure is quite different from those of other known HOs.Keywords: biliverdin; Drosophila melanogaster; heme oxygenase; insect; NADPH/cytochrome P450 reductase.Heme oxygenase (HO, EC 1.14.99.3) was first characterized in mammals as a microsomal enzyme that catalyzes the three-step oxidation of hemin to biliverdin IXa, CO, and free iron, via a-meso-hydroxyhemin, verdoheme, and ferric iron-biliverdin complex [1-3] (Scheme 1). To date two mammalian isozymes of HO have been identified [4]: HO-1, an inducible enzyme that is highly expressed in the spleen and liver; HO-2, a constitutive enzyme found abundantly in the brain and testes. The two isozymes have about 43% similarity at amino acid level, and both have a C-terminal hydrophobic domain that is involved in binding to microsomal membrane. Both HO-1 and HO-2 have been demonstrated to play important roles in physiological iron homeostasis [5,6], antioxidant defense [7,8], and possibly the cGMP signaling pathway [9,10]. Although HO-3 was once reported as an isozyme of HO, its function is not yet well defined [11].HO has also been found and characterized in bacteria [12][13][14] and plants [15][16][17][18] and other species such as Rhodophyta [19]. In contrast with mammalian HO, these HOs are water-soluble enzymes because they lack a membrane-anchoring domain at the C-termini of their sequences. In pathogenic bacteria, HO is thought to help bacteria to acquire iron from heme-containing proteins found in their host cells for survival and toxin production. In plants, biliverdin is used for the biosynthesis of photoresponsive bilins such as phycobilins and phytochromobilins [15][16][17][18][19]. Although the HOs have been characterized structurally and functional...

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[7] Preparation and characterization of insect hemoglobins from Chironomus thummi thummi

Cited by 10 publications

References 46 publications

Solution ¹H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Solution ¹H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Chironomid Midges (Diptera, Chironomidae) Show Extremely Small Genome Sizes

Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied

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[7] Preparation and characterization of insect hemoglobins from Chironomus thummi thummi

Cited by 10 publications

References 46 publications

Solution 1H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Solution 1H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Chironomid Midges (Diptera, Chironomidae) Show Extremely Small Genome Sizes

Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied

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Solution ¹H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi

Solution ¹H‐NMR Structure of the Heme Cavity in the Low‐Affinity State for the Allosteric Monomeric Cyano‐Met Hemoglobins from Chironomus thummi thummi