Sediment Transport by the Terebellid Polychaete, Amphitrite ornata (Leidy), Under Laboratory Conditions
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چکیده
منابع مشابه
Sediment Transport in Unsteady Flow Conditions
Sediment transport under unsteady flow condition is studied experimentally. In the first step, sediment transport under different steady flow conditions was measured and an empirical equation was derived for its calculation. In the next step, two continuous and three stepwise hydrographs were generated in the flume, and their sediment transport rate was measured. The continuous hydrographs were...
متن کاملEnzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding.
Amphitrite ornata dehaloperoxidase (DHP) is a heme enzyme with a globin structure, which is capable of oxidizing para-halogenated phenols to the corresponding quinones. Cloning, high-level expression, and purification of recombinant DHP are described. Recombinant DHP was assayed by stopped-flow experiments for its ability to oxidatively debrominate 2,4,6-tribromophenol (TBP). The enzymatic acti...
متن کاملPeroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata
The marine globin dehaloperoxidase-hemoglobin (DHP) from Amphitrite ornata was found to catalyze the H2O2-dependent oxidation of monohaloindoles, a previously unknown class of substrate for DHP. Using 5-Br-indole as a representative substrate, the major monooxygenated products were found to be 5-Br-2-oxindole and 5-Br-3-oxindolenine. Isotope labeling studies confirmed that the oxygen atom incor...
متن کاملThe pH dependence of the activity of dehaloperoxidase from Amphitrite ornata.
Dehaloperoxidase (DHP) from the terebellid polychaete, Amphitrite ornata, is the first hemoglobin that has peroxidase activity as part of its native function. The substrate 2,4,6-tribromophenol (TBP) is oxidatively debrominated by DHP to form 2,6-dibromoquinone (DBQ) in a two-electron process. There is a well-defined internal binding site for TBP above the heme, a feature not observed in other ...
متن کاملSubstrate binding triggers a switch in the iron coordination in dehaloperoxidase from Amphitrite ornata: HYSCORE experiments.
We have explored the effect of substrate binding on the heme iron conformation in the enzyme dehaloperoxidase (DHP) that was first isolated from the terebellid polychaete Amphitrite ornata and is now expressed in Escherichia coli.1-3 DHP is a dimeric hemoglobin4 that also has significant peroxidase activity under physiological conditions.5 Since hemoglobins and peroxidases require ferrous and f...
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ژورنال
عنوان ژورنال: Northeast Gulf Science
سال: 1983
ISSN: 0148-9836
DOI: 10.18785/negs.0602.10