Literature summary for 1.14.13.236 extracted from

Schwartz, J.K.; Wei, P.P.; Mitchell, K.H.; Fox, B.G.; Solomon, E.I.
Geometric and electronic structure studies of the binuclear nonheme ferrous active site of toluene-4-monooxygenase: parallels with methane monooxygenase and insight into the role of the effector proteins in O2 activation (2008), J. Am. Chem. Soc., 130, 7098-7109.

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Organism

Organism	UniProt	Comment	Textmining
Pseudomonas mendocina	Q00456 and Q00457 and Q00460	Q00456, Q00457 an Q00460 are components TmoA, TmoB and TmoE of diiron hydroxylase T4MOH, respectively	-
Pseudomonas mendocina KR1	Q00456 and Q00457 and Q00460	Q00456, Q00457 an Q00460 are components TmoA, TmoB and TmoE of diiron hydroxylase T4MOH, respectively	-

Cofactor

Cofactor	Comment	Organism	Structure
iron-sulfur centre	study of the Fe(II)Fe(II) active site in the hydroxylase component of toluene-4 monoxygenase and the complex of T4moH bound by its effector protein, T4moD. Binding of the effector protein changes the geometry of one iron center and orientation of its redox active orbital to accommodate the binding of O2 in a bridged structure for efficient 2-electron transfer that can form a peroxo intermediate	Pseudomonas mendocina

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Release 2023.1 (January 2023)