ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2011
A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 27 citations in OpenAlex.
- Extremophilic hemoglobins: The structure of Shewanella benthica truncated hemoglobin N.The Journal of biological chemistry · 2025Article
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- Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility.Journal of inorganic biochemistry · 2020Article
- Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1.Journal of inorganic biochemistry · 2019Article
- Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii.Biochimica et biophysica acta. General subjects · 2018Article
- Covalent attachment of the heme to Synechococcus hemoglobin alters its reactivity toward nitric oxide.Journal of inorganic biochemistry · 2017Article
- Evolutionary and Functional Relationships in the Truncated Hemoglobin Family.PLoS computational biology · 2016Article
- Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated hemoglobin with a rare histidine-lysine heme ligation.Acta crystallographica. Section F, Structural biology communications · 2015Article
- A bioinformatics insight to rhizobial globins: gene identification and mapping, polypeptide sequence and phenetic analysis, and protein modeling.F1000Research · 2015Article
- Functional and Spectroscopic Characterization of Chlamydomonas reinhardtii Truncated Hemoglobins.PloS one · 2015Article
- Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand.Biochemistry · 2014Article
- Hemoglobin: a nitric-oxide dioxygenase.Scientifica · 2012Review
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3 authors at 3 institutions in 1 country.
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Abstract
Truncated hemoglobins (trHbs) are distributed from bacteria to unicellular eukaryotes and have roles in oxygen transport and nitric oxide detoxification. It is known that trHbs exist in ciliates of the Tetrahymena group, but trHb structure and function remain poorly understood. To investigate trHb function with respect to stability of bound oxygen and protein structure, we measured the oxygen binding kinetics of Tetrahymena pyriformis trHb, and determined the crystal structure of the protein. The O(2) association and dissociation rate constants of T. pyriformis trHb were 5.5 μM(-1 )s(-1) and 0.18 s(-1), respectively. The autooxidation rate constant was 3.8 × 10(-3) h(-1). These values are similar to those of HbN from Mycobacterium tuberculosis. The three-dimensional structure of an Fe(II)-O(2) complex of T. pyriformis trHb was determined at 1.73-Å resolution. Tyr25 (B10) and Gln46 (E7) were hydrogen-bonded to a heme-bound O(2) molecule. Tyr25 donated a hydrogen bond to the terminal oxygen atom, whereas Gln46 hydrogen-bonded to the proximal oxygen atom. Furthermore, Tyr25 was hydrogen-bonded to the Gln46 and Gln50 (E11) residues. Mutations at Tyr25, Gln46, and Gln50 increased the O(2) dissociation and autooxidation rate constants. An Fe(III)-H(2)O complex of T. pyriformis trHb was formed following reaction of the Fe(II)-O(2) complex of T. pyriformis trHb, in a crystal state, with nitric oxide. This suggests that T. pyriformis trHb functions in nitric oxide detoxification.
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