Remarkable Aliphatic Hydroxylation by the Diiron Enzyme Toluene 4-Monooxygenase in Reactions with Radical or Cation Diagnostic Probes Norcarane, 1,1-Dimethylcyclopropane, and 1,1-Diethylcyclopropane†

Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15688-15701 ◽  
Author(s):  
Luke A. Moe ◽  
Zhengbo Hu ◽  
Dayi Deng ◽  
Rachel N. Austin ◽  
John T. Groves ◽  
...  
Keyword(s):  
Diiron Enzyme

Purple acid phosphatase: a diiron enzyme that catalyzes a direct phospho group transfer to water

1993 ◽  
Vol 115 (7) ◽  
pp. 2974-2975 ◽  
Author(s):  
Eugene G. Mueller ◽  
Michael W. Crowder ◽  
Bruce A. Averill ◽  
Jeremy R. Knowles
Keyword(s):  
Acid Phosphatase ◽  
Purple Acid Phosphatase ◽  
Group Transfer ◽  
Diiron Enzyme

scholarly journals Spectroscopy and DFT Calculations of a Flavo-diiron Enzyme Implicate New Diiron Site Structures

2017 ◽  
Vol 139 (34) ◽  
pp. 12009-12019 ◽  
Author(s):  
Andrew C. Weitz ◽  
Nitai Giri ◽  
Jonathan D. Caranto ◽  
Donald M. Kurtz ◽  
Emile L. Bominaar ◽  
...  
Keyword(s):  
Dft Calculations ◽  
Diiron Enzyme ◽  
Diiron Site

Density Functional Study on Possible Peroxo Form of Non-heme Diiron Enzyme Model

1997 ◽  
Vol 26 (7) ◽  
pp. 587-588 ◽  
Author(s):  
Kazunari Yoshizawa ◽  
Yasunori Yokomichi ◽  
Yoshihito Shiota ◽  
Takehiro Ohta ◽  
Tokio Yamabe
Keyword(s):  
Density Functional ◽  
Functional Study ◽  
Density Functional Study ◽  
Enzyme Model ◽  
Diiron Enzyme

Reactions of the Diiron Enzyme Stearoyl-Acyl Carrier Protein Desaturase

2004 ◽  
Vol 37 (7) ◽  
pp. 421-429 ◽  
Author(s):  
Brian G. Fox ◽  
Karen S. Lyle ◽  
Corina E. Rogge
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Diiron Enzyme

scholarly journals Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin

2020 ◽  
Vol 6 (17) ◽  
pp. eaay9226
Author(s):  
John Royer ◽  
John Shanklin ◽  
Nathalie Balch-Kenney ◽  
Maria Mayorga ◽  
Peter Houston ◽  
...  
Keyword(s):  
Double Bond ◽  
Biosynthetic Pathway ◽  
Catalytic Cycle ◽  
Carotenoid Pigments ◽  
Double Bonds ◽  
Plant Kingdom ◽  
Multifunctional Enzyme ◽  
Type Integral ◽  
Diiron Enzyme ◽  
Β Carotene

Rhodoxanthin is a vibrant red carotenoid found across the plant kingdom and in certain birds and fish. It is a member of the atypical retro class of carotenoids, which contain an additional double bond and a concerted shift of the conjugated double bonds relative to the more widely occurring carotenoid pigments, and whose biosynthetic origins have long remained elusive. Here, we identify LHRS (Lonicera hydroxylase rhodoxanthin synthase), a variant β-carotene hydroxylase (BCH)–type integral membrane diiron enzyme that mediates the conversion of β-carotene into rhodoxanthin. We identify residues that are critical to rhodoxanthin formation by LHRS. Substitution of only three residues converts a typical BCH into a multifunctional enzyme that mediates a multistep pathway from β-carotene to rhodoxanthin via a series of distinct oxidation steps in which the product of each step becomes the substrate for the next catalytic cycle. We propose a biosynthetic pathway from β-carotene to rhodoxanthin.

Threonine 201 in the Diiron Enzyme Toluene 4-Monooxygenase Is Not Required for Catalysis†

Biochemistry ◽  
2000 ◽  
Vol 39 (4) ◽  
pp. 791-799 ◽  
Author(s):  
Jeremie D. Pikus ◽  
Kevin H. Mitchell ◽  
Joey M. Studts ◽  
Kevin McClay ◽  
Robert J. Steffan ◽  
...  
Keyword(s):  
Diiron Enzyme
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