Download MendeleyLysine 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. We inspected properties of the globin domains prepared by recombinant means through site-directed mutagenesis, electronic absorption, CD, and NMR spectroscopies, and X-ray crystallography. Recombinant THB3, which lacks the proximal histidine but has a distal histidine, binds heme weakly. NMR data demonstrate that the recombinant domains of THB2 and THB4 coordinate the ferrous heme iron with the proximal histidine and a lysine from the distal helix. An X-ray structure of ferric THB4 confirms lysine coordination. THB1, THB2, and THB4 have reduction potentials between -65 and -100 mV, are capable of nitric oxide dioxygenation, are reduced at different rates by the diaphorase domain of C. reinhardtii nitrate reductase, and show different response to peroxide treatment. Three single-domain C. reinhardtii hemoglobins use lysine as a distal heme ligand in both Fe(III) and Fe(II) oxidation states. This common feature is likely related to enzymatic activity in the management of reactive oxygen species. Primary structure analysis of hemoglobins has limited power in the prediction of heme ligation. Experimental determination reveals variations in this essential property across the superfamily.
Organizational Affiliation:
T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States.
