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Microbiology 153 (2007), 3548-3562; DOI  10.1099/mic.0.2007/007930-0
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Microbiology 153 (2007), 3548-3562; DOI  10.1099/mic.0.2007/007930-0
© 2007 Society for General Microbiology

Insight into the haem d1 biosynthesis pathway in heliobacteria through bioinformatics analysis

Jin Xiong1, Carl E. Bauer2 and Anjly Pancholy1

1 Department of Biology, Texas A&M University, College Station, TX 77843, USA
2 Department of Biology, Indiana University, Bloomington, IN 47405, USA

Correspondence
Jin Xiong
jxiong{at}mail.bio.tamu.edu

Haem d1 is a unique tetrapyrrole molecule that serves as a prosthetic group of cytochrome cd1, which reduces nitrite to nitric oxide during the process of denitrification. Very little information is available regarding the biosynthesis of haem d1. The extreme difficulty in studying the haem d1 biosynthetic pathway can be partly attributed to the lack of a theoretical basis for experimental investigation. We report here a gene cluster encoding enzymes involved in the biosynthesis of haem d1 in two heliobacterial species, Heliobacillus mobilis and Heliophilum fasciatum. The gene organization of the cluster is conserved between the two species, and contains a complete set of genes that lead to the biosynthesis of uroporphyrinogen III and genes thought to be involved in the late steps of haem d1 biosynthesis. Detailed bioinformatics analysis of some of the proteins encoded in the gene cluster revealed important clues to the precise biochemical roles of the proteins in the biosynthesis of haem d1, as well as the membrane transport and insertion of haem d1 into an apocytochrome during the maturation of cytochrome cd1.

Abbreviations: ABC, ATP-binding cassette; HMM, hidden Markov model; HTH, helix–turn–helix; Lrp, leucine-responsive regulatory; PDB, Protein Data Bank; PRSS, probability of random shuffles; SAH, S-adenosyl homocysteine; SAM, S-adenosylmethionine

The GenBank/EMBL/DDBJ accession numbers for the sequences determined in this study are EU052681 and EU068732.






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