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    Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand

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    Authors
    Johnson, Eric A.
    Rice, Selena L.
    Preimesberger, Matthew R.
    Nye, Dillon B.
    Gilevicius, Lukas
    Wenke, Belinda B.
    Brown, Jason
    Witman, George B.
    Lecomte, Juliette T. J.
    UMass Chan Affiliations
    Department of Cell and Developmental Biology
    Document Type
    Journal Article
    Publication Date
    2014-07-22
    Keywords
    Chlamydomonas reinhardtii
    Chloroplast Proteins
    Gene Expression Regulation, Plant
    Heme
    Hemoglobins
    Hydrogen-Ion Concentration
    Lysine
    Nitric Oxide
    Nitrogen
    Algae
    Amino Acids, Peptides, and Proteins
    Biochemical Phenomena, Metabolism, and Nutrition
    Biochemistry
    Chemical Actions and Uses
    Genetic Phenomena
    Inorganic Chemicals
    Investigative Techniques
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    Abstract
    The nuclear genome of the model organism Chlamydomonas reinhardtii contains genes for a dozen hemoglobins of the truncated lineage. Of those, THB1 is known to be expressed, but the product and its function have not yet been characterized. We present mutagenesis, optical, and nuclear magnetic resonance data for the recombinant protein and show that at pH near neutral in the absence of added ligand, THB1 coordinates the heme iron with the canonical proximal histidine and a distal lysine. In the cyanomet state, THB1 is structurally similar to other known truncated hemoglobins, particularly the heme domain of Chlamydomonas eugametos LI637, a light-induced chloroplastic hemoglobin. Recombinant THB1 is capable of binding nitric oxide (NO(*)) in either the ferric or ferrous state and has efficient NO(*) dioxygenase activity. By using different C. reinhardtii strains and growth conditions, we demonstrate that the expression of THB1 is under the control of the NIT2 regulatory gene and that the hemoglobin is linked to the nitrogen assimilation pathway.
    Source

    Biochemistry. 2014 Jul 22;53(28):4573-89. doi: 10.1021/bi5005206. Link to article on publisher's site.

    DOI
    10.1021/bi5005206
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/26463
    PubMed ID
    24964018
    Related Resources

    Link to Article in PubMed

    Rights

    Open access via the ACS AuthorChoice + 12, Open Access option on 06/25/2015.

    ae974a485f413a2113503eed53cd6c53
    10.1021/bi5005206
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