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. 2017 Feb 13;2(2):536–545. doi: 10.1021/acsomega.6b00521

Table 1. Cu–Ligand Bond Lengths (Å) for the Active Site of LPMO.

state Cun (spin) Cu–NHis86ε Cu–NHisl Cu–NHis1δ Cu–OTyr175 Cu–OW229 Cu–OW230
1fixed CuII S = 1/2 2.02 2.07 1.98 2.80 2.28 2.11
1free CuII S = 1/2 2.03 2.03 1.99 2.34 2.83 2.03
1free,a CuII S = 1/2 2.02 2.02 1.97 2.48 3.00 2.06
1free,b CuII S = 1/2 2.04 1.98 2.02 2.47 2.96 2.07
1(42) CuII S = 1/2 1.99 2.08 1.99 3.08   2.33
1(31),c CuI S = 1/2 1.99 2.07 1.98   2.22 2.12
2fixed CuI S = 0 1.97 2.11 1.99 2.87 2.30 3.01
2free CuI S = 0 1.95 2.08 1.96 3.03 2.28 3.02
2free,a CuI S = 0 1.93 2.09 1.93 3.05 2.54 3.03
2free,b CuI S = 0 1.97 1.97 1.95 2.90 2.74 3.04
2(42) CuI S = 0 1.93 2.14 1.93 4.37 2.19  
2(41) CuI S = 0 1.91 2.27 1.91 3.23 3.32 3.11
2(31),c CuI S = 0 1.98 2.18 1.98      
2YET(8) CuI/II S = 0, 1/2 2.32 2.10 2.43 2.80 2.65 2.23
3ZUD(8) CuI/II S = 0, 1/2 2.03 2.20 1.91 2.92 2.89  
4EIR(27) CuI/II S = 0, 1/2 1.99 2.25 1.92 2.76   1.84
5ACF(56) CuI/II S = 0, 1/2 2.06 1.88 2.16 2.47    
4ALC(31),c CuII S = 1/2 1.97 2.12 1.99   2.21 2.19
4ALT(31),c CuI S = 0 1.91 2.19 1.94      
a

Optimized with TPSS-D3/def2-TZVPD.

b

Optimized with B3LYP-D3/def2-TZVPD.

c

This is from an AA10 LPMO enzyme, whose reduction in the X-ray beam has been carefully followed.