Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 55-63 |
| Seitenumfang | 9 |
| Fachzeitschrift | Biological chemistry |
| Jahrgang | 391 |
| Ausgabenummer | 1 |
| Publikationsstatus | Veröffentlicht - 1 Jan. 2010 |
Abstract
During heme biosynthesis the oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of the two propionate side chains on rings A and B of coproporphyrinogen III to the corresponding vinyl groups to yield protoporphyrinogen IX. Here, the sequence of the two decarboxylation steps during HemN catalysis was investigated. A reaction intermediate of HemN activity was isolated by HPLC analysis and identified as monovinyltripropionic acid porphyrin by mass spectrometry. This monovinylic reaction intermediate exhibited identical chromatographic behavior during HPLC analysis as harderoporphyrin (3-vinyl-8,13,17-tripropionic acid-2,7,12,18- tetramethylporphyrin). Furthermore, HemN was able to utilize chemically synthesized harderoporphyrinogen as substrate and converted it to protoporphyrinogen IX. These results suggest that during HemN catalysis the propionate side chain of ring A of coproporphyrinogen III is decarboxylated prior to that of ring B.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Klinische Biochemie
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in: Biological chemistry, Jahrgang 391, Nr. 1, 01.01.2010, S. 55-63.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX
AU - Rand, Katrin
AU - Noll, Claudia
AU - Schiebel, Hans Martin
AU - Kemken, Dorit
AU - Dülcks, Thomas
AU - Kalesse, Markus
AU - Heinz, Dirk W.
AU - Layer, Gunhild
N1 - Funding Information: We thank Prof. Jean-Charles Deybach and Caroline Schmitt (University of Paris VII, France) for the gift of plasmids pGEX-2T:CPO and pGEX-2T:CPO(R401K). We would like to thank Prof. Dieter Jahn for continuous support and helpful discussions. This work was supported by grants from the Deutsche Forschungsgemeinschaft to D.W.H. and by the Emmy-Noether-Program of the Deutsche For-schungsgemeinschaft to G.L. Funds from the Fonds der Chemischen Industrie are gratefully acknowledged by G.L. and D.W.H.
PY - 2010/1/1
Y1 - 2010/1/1
N2 - During heme biosynthesis the oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of the two propionate side chains on rings A and B of coproporphyrinogen III to the corresponding vinyl groups to yield protoporphyrinogen IX. Here, the sequence of the two decarboxylation steps during HemN catalysis was investigated. A reaction intermediate of HemN activity was isolated by HPLC analysis and identified as monovinyltripropionic acid porphyrin by mass spectrometry. This monovinylic reaction intermediate exhibited identical chromatographic behavior during HPLC analysis as harderoporphyrin (3-vinyl-8,13,17-tripropionic acid-2,7,12,18- tetramethylporphyrin). Furthermore, HemN was able to utilize chemically synthesized harderoporphyrinogen as substrate and converted it to protoporphyrinogen IX. These results suggest that during HemN catalysis the propionate side chain of ring A of coproporphyrinogen III is decarboxylated prior to that of ring B.
AB - During heme biosynthesis the oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of the two propionate side chains on rings A and B of coproporphyrinogen III to the corresponding vinyl groups to yield protoporphyrinogen IX. Here, the sequence of the two decarboxylation steps during HemN catalysis was investigated. A reaction intermediate of HemN activity was isolated by HPLC analysis and identified as monovinyltripropionic acid porphyrin by mass spectrometry. This monovinylic reaction intermediate exhibited identical chromatographic behavior during HPLC analysis as harderoporphyrin (3-vinyl-8,13,17-tripropionic acid-2,7,12,18- tetramethylporphyrin). Furthermore, HemN was able to utilize chemically synthesized harderoporphyrinogen as substrate and converted it to protoporphyrinogen IX. These results suggest that during HemN catalysis the propionate side chain of ring A of coproporphyrinogen III is decarboxylated prior to that of ring B.
KW - Escherichia coli
KW - Heme biosynthesis
KW - Oxidative decarboxylation
UR - http://www.scopus.com/inward/record.url?scp=75149117709&partnerID=8YFLogxK
U2 - 10.1515/BC.2010.006
DO - 10.1515/BC.2010.006
M3 - Article
C2 - 19919179
AN - SCOPUS:75149117709
VL - 391
SP - 55
EP - 63
JO - Biological chemistry
JF - Biological chemistry
SN - 1431-6730
IS - 1
ER -