At slow scan rates there should be no separation between the oxidative and reductive peaks.
* A one-electron site (e.g. a heme or FeS cluster) gives a broad peak (fig 1A). The equation that gives the shape and intensity of the peak is:
: Ideally, the peak position is  in both directions. The peak current is  (it is proportional to scan rate, , and to the amount of redox sites on the electrode, ). The ideal half width at half height (HWHH) equates  mV at 20 °C. Non-ideal behaviour may result in the peak being broader than the ideal limit.
* The peak shape for a two-electron redox site (e.g. a flavin) depends on the stability of the half-reduced state (fig 1B). If the half-reduced state is stable over a large range of electrode potential, the signal is the sum of two one-electron peaks (purple line in fig 1B). If the half reduced state is unstable, the signal is a single peak (red line in fig 1B), which may have up to four times the height and half the width of a one-electron peak.
* A protein that contains multiple redox centers should give multiple peaks which all have the same area (scaled by ).