Replacement of lysine 45 by uncharged residues modulates the redox-bohr effect in tetraheme...

Focuses on the use of the site-directed mutagenesis of charged residues in the vicinity of heme I, to investigate the structural basis for the pH dependence of the redox potential in the tetrahemic Desulfovibrio vulgaris cytochrome. Performance of the mutation of lysine 45, located in the neighborhood of the propionates of heme I; Indication of electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) data.