Electron transfer to the active site of the bacterial nitric oxide reductase is controlled by ligand binding to heme b

• Published in: Biochimica et biophysica acta Vol. 1807; no. 4; pp. 451 - 457
• Main Authors: Field, Sarah J, Roldan, M. Dolores, Marritt, Sophie J, Butt, Julea N, Richardson, David J, Watmough, Nicholas J
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2011
• Subjects: active sites; Catalytic Domain; electron transfer; Electron Transport; electrons; heme; Heme - chemistry; Heme - metabolism; heme iron; Hydrogen-Ion Concentration; Ligands; nitric oxide; Oxidation-Reduction; Oxidoreductases - chemistry; Oxidoreductases - metabolism; Paracoccus denitrificans; Paracoccus denitrificans - enzymology
• ISSN: 0005-2728; 0006-3002; 1879-2650
• DOI: 10.1016/j.bbabio.2011.01.009

The active site of the bacterial nitric oxide reductase from Paracoccus denitrificans contains a dinuclear centre comprising heme b₃ and non heme iron (FeB). These metal centres are shown to be at isopotential with midpoint reduction potentials of Eₘ≈+80mV. The midpoint reduction potentials of the other two metal centres in the enzyme, heme c and heme b, are greater than the dinuclear centre suggesting that they act as an electron receiving/storage module. Reduction of the low-spin heme b causes structural changes at the dinuclear centre which allow access to substrate molecules. In the presence of the substrate analogue, CO, the midpoint reduction potential of heme b₃ is raised to a region similar to that of heme c and heme b. This leads us to suggest that reduction of the electron transfer hemes leads to an opening of the active site which allows substrate to bind and in turn raises the reduction potential of the active site such that electrons are only delivered to the active site following substrate binding.