Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand.
Biochemistry
; 53(28): 4573-89, 2014 Jul 22.
Article
em En
| MEDLINE
| ID: mdl-24964018
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(â¢)) in either the ferric or ferrous state and has efficient NO(â¢) 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.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hemoglobinas
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Chlamydomonas reinhardtii
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Regulação da Expressão Gênica de Plantas
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Proteínas de Cloroplastos
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Lisina
/
Nitrogênio
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2014
Tipo de documento:
Article