Proteins with heme cofactors perform a variety of biochemical functions, including small molecule binding, which are controlled by the redox properties and chemical environments of their Fe centers. Cytochromes c’ are a class of bacterial heme proteins that bind nitric oxide (NO) and are believed to protect bacteria from nitrosative stress. In the case of <i>Alcaligenes xylosoxidans </i>cytochrome c’ (AXCP), access to the empty distal Fe site is prevented by the bulky hydrophobic Leu16 residue which is situated over the Fe center. Whereas ligand binding to ferrous AXCP has been extensively studied, the ferric state of native AXCP has received less attention since it is much less reactive. By mutating Leu16 to residues of equal or smaller size, the influence of the distal heme environment on AXCP ferric heme coordination was investigated using spectroscopic and kinetic techniques.

Distal heme coordination in ferric cytochrome c'

251st National Meeting (2016)

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