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Walter G. Zumft
Nitrate and nitric oxide, in addition to being respiratory substrates, are signal molecules for the induction of N-oxide-metabolizing enzymes. The NO signal is processed by transcription factors of the Crp-Fnr superfamily. Denitrification is intimately related to other cellular processes such as primary and secondary transport, protein translocation, cytochrome c biogenesis, anaerobic and N-oxide-dependent gene regulation, metalloprotein assembly, and the biosynthesis of cofactors. Thus, the research topic provides a fascinating area for interdisciplinary approaches Full Professor. Microbiology since 1982. Biology diploma 1968, Doctoral degree 1970, Habilitation 1974, Assoc. Professor 1980, University of
Erlangen-Nürnberg. 1971-74 Research Associate,
Purdue University, West Lafayette, IN. 1978-79
Visiting Professor, University of Georgia, Athens,
GA, 1980 Visiting Scientist, Arrhenius Laboratory,
University of Stockholm.
Phone: +49-721-608-3473; Fax: -8932; e-mail:

Principal Research Interests
Denitrification provides a distinct mode of bacterial
energy conservation. It makes use of N-oxides as
terminal electron acceptors for cellular Selected Publications
bioenergetics and thereby reverses dinitrogen fixation. The process is part of the global N-cycle, Körner, H., Sofia, H., Zumft, W. G. (2003) Phylogeny of essential for all life forms. Our main research the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol. Wunsch, P., Herb, M., Wieland, H., Schiek, U., and Zumft, W. G. (2003) Requirements for CuA and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida. J. Bacteriol., 185:887-896. 3. Zumft, W. G. (2002) Nitric oxide signaling and NO dependent transcriptional control in bacterial denitrification by members of the Fnr-Crp regulator family. J. Mol. Microbiol. Biotechnol., 4:277-286. Alvarez, M. L., Ai, J., Zumft, W. G., Sanders-Loehr, J., Dooley, D. M. (2001) Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance The activation and enzymatic transformation of N- Raman spectroscopy: evidence for sulfur coordination in the catalytic cluster. J. Am. Chem. Soc., 123:576-587. oxides is based on Fe, Cu, and Mo and their redox Charnock, J., Dreusch, A. Körner, H., Neese, F., Nelson, J., chemistry. The metal ions are found in the Kannt, A., Michel, H., Garner, D., Kroneck, P. M. H., denitrification enzymes in distinct organic cofactors Zumft, W. G. (2000) Structural investigations of the CuA or as protein-bound metal clusters. We have center of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption isolated the novel enzymes nitric oxide reductase spectroscopy. Eur. J. Biochem., 267:1368-1381. and nitrous oxide reductase, and provided their first Härtig, E., Schiek, U., Vollack, K-U., Zumft, W. G. (1999) biochemical characterization and access to the Nitrate and nitrite control of respiratory nitrate reduction in genetic basis of the process. Around 40 genes are denitrifying Pseudomonas stutzeri by a two-component regulatory system homologous to NarXL of Escherichia required to encode the core structures of the coli. J. Bacteriol., 181:3658-3665. Zumft, W. G. (1997) Cell biology and molecular basis of We are investigating the components of the denitrification. Microbiol. Mol. Biol. Rev., 61:533-616. process, their topology with respect to the bacterial cytoplasmic membrane, and their regulation.


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