Iron (II) basket-handle porphyrins (BHP) are a series of encumbered heme models designed several years ago to mimic the ligand binding site of hemoproteins. Contrary to expectations, kinetic investigations have revealed that the k(on) rates for CO and/or O-2 binding were only marginally affected by the assumed central steric hindrance of the iron atom. Thus, it was hypothesized that the internal dynamics of the molecule might be at the origin of the poor steric protection. To address this issue, measurements of nuclear magnetic resonance relaxation rates, fluorescence anisotropy experiments, and molecular dynamics simulations were undertaken. The size of BHP is small enough to allow the simulation in explicit chloroform with an almost complete sampling of the conformational space. The order parameters calculated from the MD trajectory compare well with the NMR experimental data and the predicted rotational correlation time corresponding to the Brownian motion of the molecule is in good agreement with the fluorescence measurements. Moreover, combining the results obtained using the three techniques allows the attribution of each internal NMR correlation time to a particular internal motion, revealing that even such medium-sized molecules are able to display quite complex internal dynamics. In particular, the handle phenyls that were assumed to sandwich the porphyrin have in fact a vanishing probability to be found in the proximity of the iron atom. They are therefore unable to reduce ligand accessibility significantly, which may explain the behavior of the k(on) rates.