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. Author manuscript; available in PMC: 2010 Apr 5.
Published in final edited form as: Biochemistry. 2009 Feb 10;48(5):917–928. doi: 10.1021/bi801382v

Table 3.

Edge-to-Edge Distance from a Specific Tyrosine Residue to the PGIS Heme and Best Coupling Efficiency Estimated from Electron Pathway Analysis

Tyr residue edge distance (Å) best coupling value
Tyr42 20.0 3.30 × 10−8
Tyr73 17.5 4.38 × 10−7
Tyr83 6.5 3.62 × 10−4
Tyr99 7.3 2.66 × 10−6
Tyr115 5.6 1.56 × 10−5
Tyr141 12.3 1.83 × 10−5
Tyr169 10.1 4.14 × 10−5
Tyr177 8.1 2.92 × 10−4
Tyr181 8.1 8.12 × 10−4
Tyr259 6.5 3.62 × 10−4
Tyr398 14.5 4.81 × 10−6
Tyr406 16.1 2.32 × 10−7
Tyr421 21.7 6.36 × 10−8
Tyr430 13.2 1.08 × 10−4
Tyr446 3.2 2.89 × 10−2
Tyr481 9.6 4.58 × 10−4
Tyr496 21.4 9.51 × 10−9