title: Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR.
abstract: Residual dipolar couplings measured by NMR spectroscopy reveal that the rhombicity of the electronic structure of low-spin paramagnetic hemes determines their relative contribution to the preferential orientation of a protein with multiple hemes when placed in a strong magnetic field.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal. louro@itqb.unl.pt.
authors.forename: S E
authors.initials: SE
authors.lastname: Neto
authors.forename: B M
authors.initials: BM
authors.lastname: Fonseca
authors.forename: C
authors.initials: C
authors.lastname: Maycock
authors.forename: R O
authors.initials: RO
authors.lastname: Louro
mesh_terms: D045304:Cytochromes c / Q000737:chemistry*; D004583:Electrons; D006418:Heme / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D020592:Shewanella / Q000737:chemistry / Q000201:enzymology*
chemical_list: D006418:Heme; D045304:Cytochromes c