TABLE 2.

Mononuclear iron distances

Residue or group	Distance (Å) to mononuclear iron in enzyme-substrate structure (Protein Data Bank no.)
	Phe-352-Val mutant (2HMJ)	Wild type- phenanthrene (2HMK)	Phe-352-Val mutant- phenanthrene (2HML)	Wild type- anthracene (2HMM)	Phe-352-Val mutant- anthracene (2HMN)	Wild type-3- nitrotoluene (2HMO)
Asp-205 (OD1)	2.33	2.58	2.12	2.22	2.22	2.26
Asp-205 (OD2)	2.52	2.15	2.40	2.44	2.35	2.55
His-208 (NE2)	2.11	2.13	2.26	2.14	2.17	2.16
His-213 (NE2)	2.04	2.04	2.08	2.04	2.06	2.05
OHa	1.96	2.04	1.66	1.94	1.98	1.79, 2.05
Substrateb	NAd	4.17, 4.72	3.36, 3.67	4.14, 4.26	4.47, 4.54	4.46 (5.81)c

^aHydroxide ion(s) ligated to iron.

^bDistance to the hydroxylated substrate carbon(s).

^cDistance to the methyl carbon in the nonproductive conformation.

^dNA, not applicable.