Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 95:792-796 (1991)
© 1991 American Society of Plant Biologists

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
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
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 CrossRef
Right arrow Citing Articles via Web of Science (22)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bailey, B. A.
Right arrow Articles by Larson, R. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bailey, B. A.
Right arrow Articles by Larson, R. L.
Agricola
Right arrow Articles by Bailey, B. A.
Right arrow Articles by Larson, R. L.
Metabolism and Enzymology

Maize Microsomal Benzoxazinone N-Monooxygenase 1,2

Bryan A. Bailey3 and Russell L. Larson

Biochemistry and Agronomy Departments, University of Missouri, and U.S. Department of Agriculture, Agricultural Research Service, Plant Genetics Research Unit, Columbia, Missouri 65211

The benzoxazinones occur in hydroxamic acid and lactam forms in maize (Zea mays L.) tissue. The hydroxamic acid forms which possess a N-hydroxyl group are found in the highest concentration while the lactam members which lack the N-hydroxyl group occur in lower concentrations. The hydroxamic acid 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) has as its lactam counterpart 2-hydroxy-1,4-benzoxazin-3-one (HBOA). An enzyme has been identified in maize microsomal preparations which catalyzes the N-hydroxylation of HBOA to form DIBOA. The enzyme is initially observed in seedlings 2 days after imbibition which coincides with the onset of hydroxamic acid accumulation. The enzyme requires NADPH and is inhibited by sulfhydryl reagents, NADP, cytochrome c, cations, carbon monoxide, and nitrogen gas. The effect of nitrogen can be reversed by exposing the enzyme to air, while the effect of carbon monoxide can be reversed by exposing the enzyme to 450 nanometer light during the incubation period. The apparent Km values for HBOA and NADPH are 13 and 5 micromolar, respectively. The pH optimum is 7.5 and the temperature optimum for the enzyme is 35°C. A 450 nanometer absorbance peak is observed when reduced microsomal preparations are exposed to carbon monoxide which in combination with other data presented supports the hypothesis that the enzyme is a cytochrome P-450 dependent N-monooxygenase.


3 Current address: Plant Hormone Laboratory, USDA/ARS, Beltsville Agricultural Research Center, Beltsville, MD 20705.

1 Supported in part by funds to B.A.B. from Food for the 21st Century fellowship program of the University of Missouri, Columbia.

2 Cooperative investigations, Agricultural Research Service, U.S. Department of Agriculture, and Missouri Agricultural Experiment Station, Columbia, Missouri 65211. Journal Series No. 11207.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1991 by the American Society of Plant Biologists