Standard
Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. / Sibbesen, Ole; Koch, Birgit; Halkier, Barbara Ann; Møller, Birger Lindberg.
In:
Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, No. 21, 11.10.1994, p. 9740-9744.
Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
Sibbesen, O, Koch, B, Halkier, BA & Møller, BL 1994, 'Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench', Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 21, pp. 9740-9744.
APA
Sibbesen, O., Koch, B., Halkier, B. A., & Møller, B. L. (1994). Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Proceedings of the National Academy of Sciences of the United States of America, 91(21), 9740-9744.
Vancouver
Sibbesen O, Koch B, Halkier BA, Møller BL. Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Proceedings of the National Academy of Sciences of the United States of America. 1994 Oct 11;91(21):9740-9744.
Author
Sibbesen, Ole ; Koch, Birgit ; Halkier, Barbara Ann ; Møller, Birger Lindberg. / Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. In: Proceedings of the National Academy of Sciences of the United States of America. 1994 ; Vol. 91, No. 21. pp. 9740-9744.
Bibtex
@article{de26e7f806e444dcb7767720a0734a2b,
title = "Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench",
keywords = "N-HYDROXYLATION, SUBSTRATE BINDING SPECTRA, ANTIBODY INHIBITION, DYE COLUMN CHROMATOGRAPHY",
author = "Ole Sibbesen and Birgit Koch and Halkier, {Barbara Ann} and M{\o}ller, {Birger Lindberg}",
year = "1994",
month = oct,
day = "11",
language = "English",
volume = "91",
pages = "9740--9744",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "21",
}
RIS
TY - JOUR
T1 - Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
AU - Sibbesen, Ole
AU - Koch, Birgit
AU - Halkier, Barbara Ann
AU - Møller, Birger Lindberg
PY - 1994/10/11
Y1 - 1994/10/11
KW - N-HYDROXYLATION
KW - SUBSTRATE BINDING SPECTRA
KW - ANTIBODY INHIBITION
KW - DYE COLUMN CHROMATOGRAPHY
M3 - Journal article
VL - 91
SP - 9740
EP - 9744
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 21
ER -
