The auxiliary [4Fe–4S] cluster of the Radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer-Reference-Cited by-同舟云学术

The auxiliary [4Fe–4S] cluster of the Radical SAM heme synthase from Methanosarcina barkeri is involved in electron transfer

Published:2016 Issue:7 Volume:7 Page:4633-4643
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Kühner Melanie¹²³⁴,Schweyen Peter⁵²³⁴,Hoffmann Martin⁵²³⁴,Ramos José Vazquez⁶⁷⁸⁴,Reijerse Edward J.⁹¹⁰⁴,Lubitz Wolfgang⁹¹⁰⁴,Bröring Martin⁵²³⁴,Layer Gunhild¹²³⁴⁶

Affiliation:

1. Institute of Microbiology

2. Technische Universität Braunschweig

3. 38106 Braunschweig

4. Germany

5. Institute of Inorganic and Analytical Chemistry

6. Institute of Biochemistry

7. Leipzig University

8. 04103 Leipzig

9. Max Planck Institute for Chemical Energy Conversion

10. 45470 Mülheim an der Ruhr

Abstract

The heme synthase AhbD catalyzes the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme during the alternative heme biosynthesis pathway.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/SC/C6SC01140C

Reference31 articles.

1. L-Methionine methyl is specifically incorporated into the C-2 and C-7 positions of the porphyrin of cytochrome c3 in a strictly anaerobic bacterium, Desulfovibrio vulgaris

2. A primitive pathway of porphyrin biosynthesis and enzymology in Desulfovibrio vulgaris

3. A whole genome view of prokaryotic haem biosynthesis