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Kinetics of a Two-Component p-Hydroxyphenylacetate Hydroxylase Explain How Reduced Flavin Is Transferred from the Reductase to the Oxygenase

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Department of Biochemistry and Center for Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok 10400, Thailand, Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Henri-Dunant Road, Bangkok 10300, Thailand, Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-06060, and School of Biological, Biomedical and Molecular Sciences, University of New England, Armidale, New South Wales 2351, Australia
Cite this: Biochemistry 2007, 46, 29, 8611–8623
Publication Date (Web):June 27, 2007
Copyright © 2007 American Chemical Society

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    p-Hydroxyphenylacetate hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) to form 3,4-dihydroxyphenylacetate (DHPA). HPAH is composed of two proteins:  a flavin mononucleotide (FMN) reductase (C1) and an oxygenase (C2). C1 catalyzes the reduction of FMN by NADH to generate reduced FMN (FMNH-) for use by C2 in the hydroxylation reaction. C1 is unique among the flavin reductases in that the substrate HPA stimulates the rates of both the reduction of FMN and release of FMNH- from the enzyme. This study quantitatively shows the kinetics of how the C1-bound FMN can be reduced and released to be used efficiently as the substrate for the C2 reaction; additional FMN is not necessary. Reactions in which O2 is rapidly mixed with solutions containing C1−FMNH- and C2 are very similar to those in which solutions containing O2 are mixed with one containing the C2−FMNH- complex. This suggests that in a mixture of the two proteins FMNH- binds more tightly to C2 and has already been completely transferred to C2 before it reacts with oxygen. Rate constants for the transfer of FMNH- from C1 to C2 were found to be 0.35 and ≥74 s-1 in the absence and presence of HPA, respectively. The reduction of cytochrome c by FMNH- was also used to measure the dissociation rate of FMNH- from C1. In the absence of HPA, FMNH- dissociates from C1 at 0.35 s-1, while with HPA present it dissociates at 80 s-1; these are the same rates as those for the transfer from C1 to C2. Therefore, the dissociation of FMNH- from C1 is rate-limiting in the intermolecular transfer of FMNH- from C1 to C2, and this process is regulated by the presence of HPA. This regulation avoids the production of H2O2 in the absence of HPA. Our findings indicate that no protein−protein interactions between C1 and C2 are necessary for efficient transfer of FMNH- between the proteins; transfer can occur by a rapid-diffusion process, with the rate-limiting step being the release of FMNH- from C1.

     This work was supported by NIH Grant GM64711 (to D.P.B.), Thailand Research Fund Grants RMU4880028 and RTA4780006, and a grant from the Faculty of Science, Mahidol University (to P.C.). J.S. was a recipient of a scholarship under the Commission on Higher Education Staff Development Project, Chulalongkorn University. T.P. is a recipient of a CHE-PhD-SW-INV scholarship from the Commission on Higher Education, Thailand. This study was also partly supported by a Research Team Strengthening Grant from BIOTECH to Skorn Mongkolsuk.

     Mahidol University.


     Chulalongkorn University.

     University of Michigan.

     University of New England.


     To whom correspondence should be addressed:  Department of Biochemistry and Center for Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand. Telephone:  662-2015596. Fax:  662-3547174. E-mail:  [email protected] (P.C.); Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606. Telephone:  734-764-9582. Fax:  734-764-3509. E-mail: [email protected] (D.P.B.).

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