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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 391, Issue 1

Issues

The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX

Katrin Rand
  • Division of Structural Biology, Helmholtz Center for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany
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/ Claudia Noll
  • Institute of Organic Chemistry, Leibniz University Hannover, Schneiderberg 1b, D-30167 Hannover, Germany
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/ Hans Martin Schiebel
  • Institute of Organic Chemistry, Technical University Braunschweig, Hagenring 30, D-38106 Braunschweig, Germany
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/ Dorit Kemken
  • Institute of Organic Chemistry, University of Bremen, Leobener Strasse, NW2, D-28359 Bremen, Germany
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/ Thomas Dülcks
  • Institute of Organic Chemistry, University of Bremen, Leobener Strasse, NW2, D-28359 Bremen, Germany
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/ Markus Kalesse
  • Institute of Organic Chemistry, Leibniz University Hannover, Schneiderberg 1b, D-30167 Hannover, Germany
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/ Dirk W. Heinz
  • Division of Structural Biology, Helmholtz Center for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany
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/ Gunhild Layer
  • Institute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany
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Published Online: 2009-11-17 | DOI: https://doi.org/10.1515/bc.2010.006

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.

Keywords: Escherichia coli; heme biosynthesis; oxidative decarboxylation

About the article

Corresponding author


Received: 2009-09-04

Accepted: 2009-09-24

Published Online: 2009-11-17

Published in Print: 2010-01-01


Citation Information: Biological Chemistry, Volume 391, Issue 1, Pages 55–63, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.006.

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