Results 121 to 130 of about 2,459 (167)

Protoporphyrinogen Oxidase-Inhibiting Herbicides

Weed Science, 1991
Several commercial and experimental herbicides such asp-nitrodiphenyl ethers, oxadiazoles, and cyclic imides inhibit protoporphyrinogen IX oxidase (Protox), the enzyme that converts protoporphyrinogen IX to protoporphyrin IX (Proto). This leads to uncontrolled autooxidation of the substrate and results in accumulation of Proto.
Stephen O. Duke, John Lydon, José M. Becerril, Timothy D. Sherman, Larry P. Lehnen, Hiroshi Matsumoto   +5 more
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Kinetics of Protoporphyrinogen Oxidase Inhibition by Diphenyleneiodonium Derivatives

Biochemistry, 1997
Protoporphyrinogen oxidase, the last enzyme of the common branch of the heme and chlorophyll pathways in plants, is the molecular target of diphenyl ether-type herbicides. These compounds inhibit the enzyme competitively with respect to the tetrapyrrole substrate, protoporphyrinogen IX.
S, Arnould, J L, Berthon, C, Hubert, M, Dias, C, Cibert, R, Mornet, J M, Camadro   +6 more
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Cloning, Sequence, and Expression of Mouse Protoporphyrinogen Oxidase

Archives of Biochemistry and Biophysics, 1995
Protoporphyrinogen oxidase (EC 1.3.3.4) is the penultimate enzyme in the heme biosynthetic pathway, catalyzing the six-electron oxidation of protoporphyrinogen to protoporphyrin. A dominantly inherited genetic deficiency in this enzyme results in the disease variegate porphyria.
T A, Dailey, H A, Dailey, P, Meissner, A R, Prasad   +3 more
openaire   +2 more sources

Protoporphyrinogen Oxidase-Inhibiting Herbicides

2010
Publisher Summary Protoporphyrinogen oxidase-inhibiting herbicides, also referred to as Protox- or PPO-inhibiting herbicides, were commercialized in the 1960s. Nitrofen was the first Protox-inhibiting herbicide to be introduced for commercial use in 1964.
Franck E. Dayan, Stephen O. Duke
openaire   +1 more source

Protoporphyrinogen oxidase and porphobilinogen deaminase in variegate porphyria

European Journal of Clinical Investigation, 1986
Abstract. Two enzymes of the haem biosynthetic pathway were investigated in patients with variegate porphyria. Protoporphyrinogen oxidase in cultures of Epstein‐Barr virus transformed lymphoblasts from twenty‐seven patients showed a mean maximal velocity (Vmax) of 0·39 ± 0·08+ nmol of protoporphyrin mg protein‐1 h‐1, a 52% reduction (P < 0·001 ...
P N, Meissner, R S, Day, M R, Moore, P B, Disler, E, Harley   +4 more
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Expression, purification, and characteristics of mammalian protoporphyrinogen oxidase

1997
Publisher Summary Studies have found that the B. subtilis , M. xanthus , and human protoporphyrinogen oxidase (PPO) complementary DNAs (cDNAs) contains an NH 3 -terminal 6-histidine (His 6 ) tag, which has greatly facilitated their purification and characterization. By using a metal-chelating matrix, it is possible to purify to apparent homogeneity
T A, Dailey, H A, Dailey
openaire   +2 more sources

Enantioselectivity of protoporphyrinogen oxidase‐inhibiting herbicides

Pesticide Science, 1994
AbstractProtoporphyrinogen oxidase (Protox) was inhibited stereoselectively by three pairs of enantiomers belonging to diphenyl ether (DPE) and pyrazole phenyl ether (PPE) herbicide classes. The (R) enantiomers were 10‐ to 44‐fold more active than the (S) enantiomers as inhibitors of Protox from barley etioplasts.
Ujjana B. Nandihalli, Mary V. Duke, John W. Ashmore, Vincent A. Musco, Robert D. Clark, Stephen O. Duke   +5 more
openaire   +1 more source

Three trifluoromethyl-substituted protoporphyrinogen IX oxidase inhibitors

Acta Crystallographica Section C Crystal Structure Communications, 2005
The structures of methyl 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoate, C15H9ClF3N3O5, (I), methyl 2-chloro-5-[3-methyl-2,6-dioxo-4-(trifluoromethyl)-1,2,3,6-tetrahydropyrimidin-1-yl]benzoate, C14H10ClF3N2O4, (II), and 2-[4-chloro-2-fluoro-5-(prop-2-ynyloxy)phenyl]-4-(trifluoromethyl)piperidine-2,6-dione, C15H10ClF4NO3, (III), are similar in ...
Bin, Li, Yu Ming, Lan, Chi Tung, Hsu, Zhen Long, Liu, Hai Bin, Song, Chao, Wu, Hua Zheng, Yang   +6 more
openaire   +2 more sources

The expression of protoporphyrinogen oxidase in human tissues.

Cellular and molecular biology (Noisy-le-Grand, France), 2013
Protoporphyrinogen oxidase is the penultimate enzyme in the haem biosynthetic pathway. In this study, the expression of protoporphyrinogen oxidase in a variety of human organs has been documented by immunohistochemical means at the light microscopy level in order to shed light on its inter- and intra-organ distribution.
A V, Corrigall, J A H, Campbell, K, Siziba, R E, Kirsch, P N, Meissner   +4 more
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Herbicidal Efficacy of Protoporphyrinogen Oxidase Inhibitors

1999
Compounds which inhibit protoporphyrinogen oxidase (Protox) were known as “photobleaching herbicides” before their site of action was discovered. Photobleaching herbicides cause very strong bleaching of the treated part of higher plants. It was known that a photobleaching herbicide requires oxygen and light to express its herbicidal activity.
openaire   +1 more source