Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii.
Johnson, E.A., Russo, M.M., Nye, D.B., Schlessman, J.L., Lecomte, J.T.J.(2018) Biochim Biophys Acta Gen Subj 1862: 2660-2673
- PubMed: 30251657 
- DOI: https://doi.org/10.1016/j.bbagen.2018.08.009
- Primary Citation of Related Structures:  
6BME - PubMed Abstract: 
The nuclear genome of Chlamydomonas reinhardtii encodes a dozen hemoglobins of the truncated lineage. Four of these, named THB1-4, contain a single ~130-residue globin unit. THB1, which is cytoplasmic and capable of nitric oxide dioxygenation activity, uses a histidine and a lysine as axial ligands to the heme iron. In the present report, we compared THB2, THB3, and THB4 to THB1 to gain structural and functional insights into algal globins.
Organizational Affiliation: 
T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States.