Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii

Article ID	Journal	Published Year	Pages	File Type
8949285	Biochimica et Biophysica Acta (BBA) - General Subjects	2018	52 Pages	PDF

Keywords

G6P pH*GlbN tris-acetate-phosphate FNR DEAE NOE NOESY TOCSY HPD THB HSQC NCS NADPH PDB NOD RMSD TLS flavin adenine dinucleotide IPTG nuclear magnetic resonance DQF-COSY Ferredoxin-NADP+ reductase nuclear overhauser effect SDS-PAGE Sodium dodecyl sulfate polyacrylamide gel electrophoresis root-mean-square deviation isopropyl β-D-1-thiogalactopyranoside FAD Tract Translation/Libration/Screw Tris-EDTA non-crystallographic symmetry diethylaminoethyl Sodium dithionite TAP nuclear Overhauser spectroscopy Total correlation spectroscopy double-quantum filtered correlation spectroscopy SAD Luria-Bertani wild-type Nitric oxide Nitric Oxide dioxygenase nicotinamide adenine dinucleotide phosphate Hemoglobin single-wavelength anomalous diffraction Protein Data Bank polyethylene glycol PEG glucose-6-phosphate one-dimensional heteronuclear single quantum coherence

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii

Authors

Eric A. Johnson, Miranda M. Russo, Dillon B. Nye, Jamie L. Schlessman, Juliette T.J. Lecomte,