Biochemistry

Pulsed EPR Study of Amino Acid and Tetrahydropterin Binding in a Tyrosine Hydroxylase Nitric Oxide Complex: Evidence for Substrate Rearrangements in the …

…, BE Eser, HR Ellis, PF Fitzpatrick, J McCracken

Index: Krzyaniak, Matthew D.; Eser, Bekir E.; Ellis, Holly R.; Fitzpatrick, Paul F.; McCracken, John Biochemistry, 2013 , vol. 52, # 47 p. 8430 - 8441

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Citation Number: 7

Abstract

Tyrosine hydroxylase is a nonheme iron enzyme found in the nervous system that catalyzes the hydroxylation of tyrosine to form l-3, 4-dihydroxyphenylalanine, the rate-limiting step in the biosynthesis of the catecholamine neurotransmitters. Catalysis requires the binding of three substrates: tyrosine, tetrahydrobiopterin, and molecular oxygen. We have used nitric oxide as an O2 surrogate to poise Fe (II) at the catalytic site in an S= 3/2,{FeNO} 7 form ...