The advantageous characteristics attributed to the ¹⁹F nucleus have made it a popular target for NMR once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle-spinning NMR to fluorine-labeled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilized to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular ¹⁹F MAS NMR often suffers from slow longitudinal <em>T</em>₁ relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton <em>T</em>₁ relaxation times, to ¹⁹F-labeled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on ¹⁹F and ¹³C <em>T</em>₁ and <em>T</em>₂ relaxation in a [5-¹⁹F¹³C]-tryptophan-labeled protein via ¹⁹F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of ¹⁹F MAS NMR experiments without compromising resolution. Additionally, we report the chemical-shift assignments of all four fluorotryptophan signals in the 12 &times; 39 kDa large protein using a mutagenesis approach.