The relaxation dynamics of 5,10,15,20-tetrakis(4-hydroxyphenyl)-porphyrin (p-THPP) in tetrahydrofuran (THF) and encapsulated within the human serum albumin (HSA) protein in water solution was investigated. The protein environment affects the B -> Q(y). and Q(x)-> Q(y) transition dynamics (from 80 and 140-200 fs in THF to 50 and 100 fs in HSA, respectively) as well as the lifetime of the relaxed Q. state (9.1 vs 9.9 ns). The most prominent differences are observed in the relaxation dynamics in the hot Q(x) state in HSA, which includes the energy transfer to the protein in similar to 1 ps and much slower solvent-assisted thermal equilibration component of about 20-30 ps.