Affiliation:
1. Department of Microbiology and Department of Biochemistry and Molecular Biology, Center for Metalloenzyme Studies, Biomedical and Health Sciences Institute, University of Georgia, Athens, Georgia 30602-7229
Abstract
ABSTRACT
The terminal enzyme of heme biosynthesis, ferrochelatase (EC 4.99.1.1), catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme. Prior to the present work, [2Fe-2S] clusters have been identified and characterized in animal ferrochelatases but not in plant or prokaryotic ferrochelatases. Herein we present evidence that ferrochelatases from the bacteria
Caulobacter crescentus
and
Mycobacterium tuberculosis
possess [2Fe-2S] clusters. The enzyme from
C. crescentus
is a homodimeric, membrane-associated protein while the enzyme from
M. tuberculosis
is monomeric and soluble. The clusters of the
C. crescentus
and
M. tuberculosis
ferrochelatases are ligated by four cysteines but possess ligand spacings that are unlike those of any previously characterized [2Fe-2S] cluster-containing protein, including the ferrochelatase of the yeast
Schizosaccharomyces pombe
. Thus, the microbial ferrochelatases represent a new group of [2Fe-2S] cluster-containing proteins.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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