Relaxation times have been obtained with time-domain EPR for the dinuclear mixed valence [CuA(1.5) ... CuA(1.5)] S = 1/2 center in nitrous oxide reductase, N2OR, from Pseudomonas stutzeri, in the Tn5 mutant defective in copper chromophore biosynthesis, in a synthetic mixed valence complex, and in type 1 and 2 copper complexes. Data confirmed that the intrinsic electron spin-lattice relaxation time, T1, for N2OR in the temperature range of 6-25 K is unusually short for copper centers. At best, a twofold increase of T1 from g_^ to g_|| was measured. Optimized fits of the saturation-recovery data were obtained using both double-exponential and  stretched-exponential functions. The temperature dependence of the spin-lattice relaxation rate of mutant N2OR is about T ^5.0 with the stretched-exponential model or T ^3.3 and T ^3.9 for the model using the sum of two exponentials. These T1s are intrinsic to the mixed valence [CuA(1.5) ... CuA(1.5)] center, and no interaction of the second copper center in wild-type N2OR with the [CuA(1.5) ... CuA(1.5)] center has been observed. The T1 of the mixed valence center of N2OR is not only shorter than for monomeric square planar Cu(II) complexes, but also shorter than for a synthetic mixed valence complex, Cu2{N[CH2CH2NHCH2CH2NHCH2CH2]3N}. The short T1 is attributed to the vibrational modes of type 1 copper and/or the metal-metal interaction in [CuA(1.5) ... CuA(1.5)].