JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Detmer, K.
Right arrow Articles by Massey, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Detmer, K.
Right arrow Articles by Massey, V.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 259, Issue 18, 11265-11272, 09, 1984

Effect of monovalent anions on the mechanism of phenol hydroxylase

K Detmer and V Massey

The mechanism of phenol hydroxylase (EC 1.14.13.7) has been studied by steady state and rapid reaction kinetic techniques. Both techniques give results consistent with the Bi Uni Uni Bi ping-pong mechanism proposed for other flavin-containing aromatic hydroxylases. The enzyme binds phenolic substrate and NADPH in that order, followed by reduction of the flavin and release of NADP+. A transient charge transfer complex between reduced enzyme and NADP+ can be detected. Molecular oxygen then reacts with the reduced enzyme-substrate complex. Two to three flavin- oxygen intermediates can be detected in the oxidative half-reaction depending on the substrate, provided monovalent anions are present. Oxygen transfer is complete with the formation of the second intermediate. Based on its UV absorption spectrum and on the fact that oxygen transfer has taken place, the last of these intermediates is presumably the flavin C(4a)-hydroxide. Monovalent anions are uncompetitive inhibitors of phenol hydroxylase. The mechanistic step most affected is the dehydration of the flavin C(4a)-hydroxide to give oxidized enzyme. Chloride also kinetically stabilizes the blue flavin semiquinone of phenol hydroxylase during photoreduction. These data suggest binding of monovalent anions results in stabilization of a proton on the N(5) position of the flavin.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
V. P. Swetha, A. Basu, and P. S. Phale
Purification and Characterization of 1-Naphthol-2-Hydroxylase from Carbaryl-Degrading Pseudomonas Strain C4
J. Bacteriol., April 1, 2007; 189(7): 2660 - 2666.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. Dai, J. B. Rogers, J. R. Warner, and S. D. Copley
A Previously Unrecognized Step in Pentachlorophenol Degradation in Sphingobium chlorophenolicum Is Catalyzed by Tetrachlorobenzoquinone Reductase (PcpD)
J. Bacteriol., January 1, 2003; 185(1): 302 - 310.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Chakraborty and V. Massey
Reaction of Reduced Flavins and Flavoproteins with Diphenyliodonium Chloride
J. Biol. Chem., October 25, 2002; 277(44): 41507 - 41516.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Meyer, A. Schmid, M. Held, A. H. Westphal, M. Rothlisberger, H.-P. E. Kohler, W. J. H. van Berkel, and B. Witholt
Changing the Substrate Reactivity of 2-Hydroxybiphenyl 3-Monooxygenase from Pseudomonas azelaica HBP1 by Directed Evolution
J. Biol. Chem., February 8, 2002; 277(7): 5575 - 5582.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. A. Suske, W. J. H. van Berkel, and H.-P. E. Kohler
Catalytic Mechanism of 2-Hydroxybiphenyl 3-Monooxygenase, a Flavoprotein from Pseudomonas azelaica HBP1
J. Biol. Chem., November 19, 1999; 274(47): 33355 - 33365.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. A. Suske, M. Held, A. Schmid, T. Fleischmann, M. G. Wubbolts, and H.-P. E. Kohler
Purification and Characterization of 2-Hydroxybiphenyl 3-Monooxygenase, a Novel NADH-dependent, FAD-containing Aromatic Hydroxylase from Pseudomonas azelaica HBP1
J. Biol. Chem., September 26, 1997; 272(39): 24257 - 24265.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.