PMID- 18973625 OWN - NLM STAT- MEDLINE DCOM- 20081217 LR - 20131121 IS - 1462-2920 (Electronic) IS - 1462-2912 (Linking) VI - 10 IP - 11 DP - 2008 Nov TI - Environmental detection of octahaem cytochrome c hydroxylamine/hydrazine oxidoreductase genes of aerobic and anaerobic ammonium-oxidizing bacteria. PG - 3140-9 LID - 10.1111/j.1462-2920.2008.01732.x [doi] AB - Bacterial aerobic ammonium oxidation and anaerobic ammonium oxidation (anammox) are important processes in the global nitrogen cycle. Key enzymes in both processes are the octahaem cytochrome c (OCC) proteins, hydroxylamine oxidoreductase (HAO) of aerobic ammonium-oxidizing bacteria (AOB), which catalyses the oxidation of hydroxylamine to nitrite, and hydrazine oxidoreductase (HZO) of anammox bacteria, which converts hydrazine to N(2). While the genomes of AOB encode up to three nearly identical copies of hao operons, genome analysis of Candidatus'Kuenenia stuttgartiensis' showed eight highly divergent octahaem protein coding regions as possible candidates for the HZO. Based on their phylogenetic relationship and biochemical characteristics, the sequences of these eight gene products grouped in three clusters. Degenerate primers were designed on the basis of available gene sequences with the aim to detect hao and hzo genes in various ecosystems. The hao primer pairs amplified gene fragments from 738 to 1172 bp and the hzo primer pairs amplified gene fragments from 289 to 876 bp in length, when tested on genomic DNA isolated from a variety of AOB and anammox bacteria. A selection of these primer pairs was also used successfully to amplify and analyse the hao and hzo genes in community DNA isolated from different ecosystems harbouring both AOB and anammox bacteria. We propose that OCC protein-encoding genes are suitable targets for molecular ecological studies on both aerobic and anaerobic ammonium-oxidizing bacteria. FAU - Schmid, Markus C AU - Schmid MC AD - Department of Microbiology, IWWR, Radboud University Nijmegen, Nijmegen, the Netherlands. mschmid@science.ru.nl FAU - Hooper, Alan B AU - Hooper AB FAU - Klotz, Martin G AU - Klotz MG FAU - Woebken, Dagmar AU - Woebken D FAU - Lam, Phyllis AU - Lam P FAU - Kuypers, Marcel M M AU - Kuypers MM FAU - Pommerening-Roeser, Andreas AU - Pommerening-Roeser A FAU - Op den Camp, Huub J M AU - Op den Camp HJ FAU - Jetten, Mike S M AU - Jetten MS LA - eng SI - GENBANK/FM163618 SI - GENBANK/FM163619 SI - GENBANK/FM163620 SI - GENBANK/FM163621 SI - GENBANK/FM163622 SI - GENBANK/FM163623 SI - GENBANK/FM163624 SI - GENBANK/FM163625 SI - GENBANK/FM163626 SI - GENBANK/FM163627 SI - GENBANK/FM163628 SI - GENBANK/FM163629 SI - GENBANK/FM163630 SI - GENBANK/FM163631 SI - GENBANK/FM163632 PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - England TA - Environ Microbiol JT - Environmental microbiology JID - 100883692 RN - 0 (Bacterial Proteins) RN - 0 (Cytochrome c Group) RN - 0 (DNA Primers) RN - 0 (DNA, Bacterial) RN - 0 (Hydrazines) RN - 27RFH0GB4R (hydrazine) RN - 2FP81O2L9Z (Hydroxylamine) RN - 9035-44-3 (cytochrome c(3)) RN - EC 1.- (Oxidoreductases) SB - IM MH - Amino Acid Sequence MH - Bacterial Proteins/*genetics MH - Cytochrome c Group/*metabolism MH - DNA Primers MH - DNA, Bacterial/chemistry/genetics MH - *Environmental Microbiology MH - Hydrazines/*metabolism MH - Hydroxylamine/*metabolism MH - Molecular Sequence Data MH - Oxidoreductases/*genetics MH - Phylogeny MH - Polymerase Chain Reaction/*methods MH - Sequence Alignment MH - Sequence Analysis, DNA EDAT- 2008/11/01 09:00 MHDA- 2008/12/18 09:00 CRDT- 2008/11/01 09:00 PHST- 2008/11/01 09:00 [pubmed] PHST- 2008/12/18 09:00 [medline] PHST- 2008/11/01 09:00 [entrez] AID - EMI1732 [pii] AID - 10.1111/j.1462-2920.2008.01732.x [doi] PST - ppublish SO - Environ Microbiol. 2008 Nov;10(11):3140-9. doi: 10.1111/j.1462-2920.2008.01732.x.